Proteopedia - User contributions [en]

Sandbox 122

2016-08-04T19:29:28Z

Allison Granberry:

==Karyopherin Beta 2 :)==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of <scene name='37/372723/4oo6_rainbow_heat_repeats/1'>20 antiparallel helices </scene>called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT]repeats. These HEAT repeats contribute to kapβ2’s large superhelical shape. That form two arches:one at the <scene name='37/372723/4oo6_ran_binding_site/2'>N-Terminal</scene> and the other at the
<scene name='37/372723/4oo6_substrate_binding_side/2'>C-Terminal</scene> Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

'''How Does Kapβ2 Recognizes Cargo In the Cytoplasm'''
:The NLS located on Kapβ2 cargos are named PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative

Recognition the PY-NLS by Kapβ2 follows a certain guidelines:
#PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
#PY-NLS hass an overall <scene name='37/372723/Positive_interaction_nls_only/3'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2.
#General sequence for the PY-NLS is either a hydrophobic or base at the motif at N-terminus and R-X2-5- P-Y motif at the C-terminus

The PY-NLS of 4OO6 contains a basic rather than hydrophobic N-terminal motif.
<scene name='37/372723/Label_nls_arg_glu_interaction/2'>Basic interactions at the N-terminal </scene> motif of the PY-NLS include: Arg92, Arg94, and Arg96 of the NLS with Glu588 and Glu496 of Kapβ2.
<scene name='37/372723/Labelcterminus_interaction_nls/1'>Interactions of the C-terminal</scene> R-X2-5- P-Y motif of the NLS include: Pro98 and Tyr99 of the NLS with Ala381,Ala382, Ala423, Ile457, and Trp460 of Kapβ2.

Upon binding Kapβ2, the NLS structure conforms to and makes contact with the internal surface of Kapβ2 C-terminal arch

Sandbox 122

2016-08-04T19:27:53Z

Allison Granberry:

==Karyopherin Beta 2 :)==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of <scene name='37/372723/4oo6_rainbow_heat_repeats/1'>20 antiparallel helices </scene>called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT]repeats. These HEAT repeats contribute to kapβ2’s large superhelical shape. That form two arches:one at the <scene name='37/372723/4oo6_ran_binding_site/2'>N-Terminal</scene> and the other at the
<scene name='37/372723/4oo6_substrate_binding_side/2'>C-Terminal</scene> Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

'''How Does Kapβ2 Recognizes Cargo In the Cytoplasm'''
:The NLS located on Kapβ2 cargos are named PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative

Recognition the PY-NLS by Kapβ2 follows a certain guidelines:
#PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
#PY-NLS hass an overall <scene name='37/372723/Positive_interaction_nls_only/2'>positive charge </scene> allowing for electrostatic compatibility with Kapβ2.
#General sequence for the PY-NLS is either a hydrophobic or base at the motif at N-terminus and R-X2-5- P-Y motif at the C-terminus

The PY-NLS of 4OO6 contains a basic rather than hydrophobic N-terminal motif.
<scene name='37/372723/Label_nls_arg_glu_interaction/2'>Basic interactions at the N-terminal </scene> motif of the PY-NLS include: Arg92, Arg94, and Arg96 of the NLS with Glu588 and Glu496 of Kapβ2.
<scene name='37/372723/Labelcterminus_interaction_nls/1'>Interactions of the C-terminal</scene> R-X2-5- P-Y motif of the NLS include: Pro98 and Tyr99 of the NLS with Ala381,Ala382, Ala423, Ile457, and Trp460 of Kapβ2.

Upon binding Kapβ2, the NLS structure conforms to and makes contact with the internal surface of Kapβ2 C-terminal arch

Sandbox 122

2016-08-04T19:14:25Z

Allison Granberry:

==Karyopherin Beta 2 :)==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of <scene name='37/372723/4oo6_rainbow_heat_repeats/1'>20 antiparallel helices </scene>called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT]repeats. These HEAT repeats contribute to kapβ2’s large superhelical shape. That form two arches:one at the <scene name='37/372723/4oo6_ran_binding_site/2'>N-Terminal</scene>and the other at the
<scene name='37/372723/4oo6_substrate_binding_side/2'>C-Terminal</scene> Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

'''How Does Kapβ2 Recognizes Cargo In the Cytoplasm'''
:The NLS located on Kapβ2 cargos are named PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative

Recognition the PY-NLS by Kapβ2 follows a certain guidelines:
#PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
#PY-NLS hass an overall positive charge allowing for electrostatic compatibility with Kapβ2.
#General sequence for the PY-NLS is either a hydrophobic or base at the motif at N-terminus and R-X2-5- P-Y motif at the C-terminus

The PY-NLS of 4OO6 contains a basic rather than hydrophobic N-terminal motif.
<scene name='37/372723/Label_nls_arg_glu_interaction/2'>Basic interactions at the N-terminal </scene> motif of the PY-NLS include: Arg92, Arg94, and Arg96 of the NLS with Glu588 and Glu496 of Kapβ2.
<scene name='37/372723/Labelcterminus_interaction_nls/1'>Interactions of the C-terminal</scene> R-X2-5- P-Y motif of the NLS include: Pro98 and Tyr99 of the NLS with Ala381,Ala382, Ala423, Ile457, and Trp460 of Kapβ2.

Upon binding Kapβ2, the NLS structure conforms to and makes contact with the internal surface of Kapβ2 C-terminal arch

Sandbox 122

2016-08-04T19:11:23Z

Allison Granberry:

==Karyopherin Beta 2 :)==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of <scene name='37/372723/4oo6_rainbow_heat_repeats/1'>20 antiparallel helices </scene>called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT]repeats. These HEAT repeats contribute to kapβ2’s large superhelical shape. That form two arches:one at the <scene name='37/372723/4oo6_ran_binding_site/1'>N-terminal </scene>and the other at the <scene name='37/372723/4oo6_substrate_binding_side/1'>C- terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

'''How Does Kapβ2 Recognizes Cargo In the Cytoplasm'''
:The NLS located on Kapβ2 cargos are named PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative

Recognition the PY-NLS by Kapβ2 follows a certain guidelines:
#PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
#PY-NLS hass an overall positive charge allowing for electrostatic compatibility with Kapβ2.
#General sequence for the PY-NLS is either a hydrophobic or base at the motif at N-terminus and R-X2-5- P-Y motif at the C-terminus

The PY-NLS of 4OO6 contains a basic rather than hydrophobic N-terminal motif.
<scene name='37/372723/Label_nls_arg_glu_interaction/2'>Basic interactions at the N-terminal </scene> motif of the PY-NLS include: Arg92, Arg94, and Arg96 of the NLS with Glu588 and Glu496 of Kapβ2.
<scene name='37/372723/Labelcterminus_interaction_nls/1'>Interactions of the C-terminal</scene> R-X2-5- P-Y motif of the NLS include: Pro98 and Tyr99 of the NLS with Ala381,Ala382, Ala423, Ile457, and Trp460 of Kapβ2.

Upon binding Kapβ2, the NLS structure conforms to and makes contact with the internal surface of Kapβ2 C-terminal arch

Sandbox 130

2016-08-04T18:58:15Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal ([https://en.wikipedia.org/wiki/Nuclear_localization_sequence NLS] or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

'''How does Kapβ2 identify its cargo?'''

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include:
<scene name='37/372730/Backbone_arg92_94_96_/1'>Arg92, Arg94, Arg96</scene> of the NLS with Glu588 and Glu496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2: Pro98 and Tyr99 of the NLS with Ala381, Ala421, Ile456, Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 130

2016-08-04T18:54:08Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal ([https://en.wikipedia.org/wiki/Nuclear_localization_sequence NLS] or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

'''How does Kapβ2 identify its cargo?'''

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include:
<scene name='37/372730/Backbone_arg92_94_96_/1'>Arg92, Arg94, Arg96</scene> of the NLS with Glu588 and Glue 496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2: Pro98 and Tyr99 of the NLS with Ala381, Ala421, Ile456, Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 122

2016-08-04T18:42:42Z

Allison Granberry:

==Karyopherin Beta 2 :)==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of <scene name='37/372723/4oo6_rainbow_heat_repeats/1'>20 antiparallel helices </scene>called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT]repeats. These HEAT repeats contribute to kapβ2’s large superhelical shape. That form two arches:one at the <scene name='37/372723/4oo6_ran_binding_site/1'>N-terminal </scene>and the other at the <scene name='37/372723/4oo6_substrate_binding_side/1'>C- terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

'''How Does Kapβ2 Recognizes Cargo In the Cytoplasm'''
:The NLS located on Kapβ2 cargos are named PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative

Recognition the PY-NLS by Kapβ2 follows a certain guidelines:
#PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
#PY-NLS hass an overall positive charge allowing for electrostatic compatibility with Kapβ2.
#General sequence for the PY-NLS is either a hydrophobic or base at the motif at N-terminus and R-X2-5- P-Y motif at the C-terminus

The PY-NLS of 4OO6 contains a basic rather than hydrophobic N-terminal motif.
<scene name='37/372723/Label_nls_arg_glu_interaction/2'>Basic interactions at the N-terminal </scene> motif of the PY-NLS include: Arg92, Arg94, and Arg96 of the NLS with Glu588 and Glu496 of Kapβ2. Interactions of the C-terminal R-X2-5- P-Y motif of the NLS include: Pro98 and Tyr99 of the NLS with Ala381, Ala42, Ile456, and Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS structure conforms to and makes contact with the internal surface of Kapβ2 C-terminal arch

Sandbox 130

2016-08-04T18:42:20Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal ([https://en.wikipedia.org/wiki/Nuclear_localization_sequence NLS] or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

'''How does Kapβ2 identify its cargo?'''

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include:
<scene name='37/372730/Backbone_arg92_94_96/2'>Arg92, Arg94, Arg96</scene> of the NLS with Glu588 and Glue 496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2: Pro98 and Tyr99 of the NLS with Ala381, Ala421, Ile456, Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 148

2016-08-04T18:21:25Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/2'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg_positive/2'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 (human) Kapβ2 contains a basic rather than a hydrophobic N-terminal motif. <scene name='37/372748/Kapb2_rainbow_nterminal_motif2/4'>Basic interactions at the N-terminal</scene> motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 148

2016-08-04T17:59:18Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/2'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg_positive/2'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 (human) Kapβ2 contains a basic rather than a hydrophobic N-terminal motif. <scene name='37/372748/Kapb2_rainbow_nterminal_motif2/3'>Basic interactions at the N-terminal</scene> motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 148

2016-08-04T17:38:39Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/2'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg_positive/2'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 (human) Kapβ2 contains a basic rather than a hydrophobic N-terminal motif. <scene name='37/372748/Kapb2_rainbow_nterminal_motif2/1'>Basic interactions at the N-terminal</scene> motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 130

2016-08-04T17:22:03Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal ([https://en.wikipedia.org/wiki/Nuclear_localization_sequence NLS] or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

'''How does Kapβ2 identify its cargo?'''

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include: Arg92, Arg94, Arg96 of the NLS with Glu588 and Glue 496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2: Pro98 and Tyr99 of the NLS with Ala381, Ala421, Ile456, Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 148

2016-08-04T17:19:49Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/2'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg_positive/1'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 (human) Kapβ2 contains a basic rather than a hydrophobic N-terminal motif. <scene name='37/372748/Kapb2_rainbow_nterminal_motif2/1'>Basic interactions at the N-terminal</scene> motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 130

2016-08-04T17:18:08Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal ([https://en.wikipedia.org/wiki/Nuclear_localization_sequence NLS] or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

'''How does Kapβ2 identify its cargo?'''
The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include: Arg92, Arg94, Arg96 of the NLS with Glu588 and Glue 496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2: Pro98 and Tyr99 of the NLS with Ala381, Ala421, Ile456, Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 148

2016-08-04T17:03:41Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/2'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg/2'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. <scene name='37/372748/Kapb2_rainbow_nterminal_motif2/1'>Basic interactions at the N-terminal</scene> motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 148

2016-08-03T19:37:13Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg/2'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. <scene name='37/372748/Kapb2_rainbow_nterminal_motif2/1'>Basic interactions at the N-terminal</scene> motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 148

2016-08-03T19:12:16Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg/2'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. <scene name='37/372748/Kapb2_rainbow_nterminal_motif/1'>Basic interactions</scene> at the N-terminal motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 148

2016-08-03T18:42:04Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall <scene name='37/372748/Kapb2_rainbow_arg/2'>positive charge</scene> allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. Basic interactions at the N-terminal motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 122

2016-08-03T18:20:31Z

Allison Granberry:

==Karyopherin Beta 2 :)==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of <scene name='37/372723/4oo6_rainbow_heat_repeats/1'>20 antiparallel helices </scene>called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT]repeats. These HEAT repeats contribute to kapβ2’s large superhelical shape. That form two arches:one at the <scene name='37/372723/4oo6_ran_binding_site/1'>N-terminal </scene>and the other at the <scene name='37/372723/4oo6_substrate_binding_side/1'>C- terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

'''How Does Kapβ2 Recognizes Cargo In the Cytoplasm'''
:The NLS located on Kapβ2 cargos are named PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative

Recognition the PY-NLS by Kapβ2 follows a certain guidelines:
#PY-NLS, when not bound to Kapβ2, lacks a secondary structure.
#PY-NLS hass an overall positive charge allowing for electrostatic compatibility with Kapβ2.
#General sequence for the PY-NLS is either a hydrophobic or base at the motif at N-terminus and R-X2-5- P-Y motif at the C-terminus

The PY-NLS of 4OO6 contains a basic rather than hydrophobic N-terminal motif. Basic interactions at the N-terminal motif of the PY-NLS include: Arg92, Arg94, and Arg96 of the NLS with Glu588 and Glu496 of Kapβ2. Interactions of the C-terminal R-X2-5- P-Y motif of the NLS include: Pro98 and Tyr99 of the NLS with Ala381, Ala42, Ile456, and Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS structure conforms to and makes contact with the internal surface of Kapβ2 C-terminal arch

Sandbox 148

2016-08-03T18:04:00Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. Basic interactions at the N-terminal motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98 and Tyr 99 of the NLS with Ala 381, Ala 421, Ile 456, Trp 459 of Kapβ2.

Sandbox 148

2016-08-03T17:59:16Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. Basic interactions at the N-terminal motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2: Pro 98,

Sandbox 130

2016-08-02T19:17:10Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal ([https://en.wikipedia.org/wiki/Nuclear_localization_sequence NLS] or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include: Arg92, Arg94, Arg96 of the NLS with Glu588 and Glue 496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 130

2016-08-02T19:16:08Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal ([https://en.wikipedia.org/wiki/Nuclear_localization_sequence] or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include: Arg92, Arg94, Arg96 of the NLS with Glu588 and Glue 496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 148

2016-08-02T19:09:13Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the [https://en.wikipedia.org/wiki/Nuclear_localization_sequence PY-NLS] and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. Basic interactions at the N-terminal motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2.

Sandbox 148

2016-08-02T19:04:32Z

Allison Granberry:

<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminal motif. Basic interactions at the N-terminal motif pf the PY-NLS include: Arg 92, Arg 94 and Arg 96 of the NLS with Glu 588 and Glu 496 of Kapβ2. Interactions of the C-terminal R-X2-5P-Y motif of the NLS include: Pro 98 of the NLS with Ile 456 and Trp 459 of Kapβ2.

Sandbox 130

2016-08-02T19:00:58Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 4OO6 contains a basic rather than a hydrophobic N-terminus motif. Basic interactions at the N-terminal motif of the PY-NLS include: Arg92, Arg94, Arg96 of the NLS with Glu588 and Glue 496 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Pro98 of NLS with Ile456 and Trp459 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

Sandbox 130

2016-08-02T17:24:06Z

Allison Granberry:

==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport ofRNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

The PY-NLS of 2H4M contains a hydrophobic rather than a basic N-terminus motif. Hydrophobic interactions at the N-terminal motif of the PY-NLS include: Phe273, Gly274, Pro275, Met276 of the NLS with Trp730 and Ile773 of Kapβ2. Interactions of the C-terminal R-X P-Y motif of the NLS include: Arg284 of the NLS with Glu509 and Asp543 of Kapβ2: Pro288 and Tyr289 of the NLS with Ala380, Ala381, Leu419, Ile457, Tro460 and Arg464 of Kapβ2.

Upon binding Kapβ2, the NLS gains structure conforms to and makes contacts with the internal surface of the Kapβ2 C-terminal arch.

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==Karyopherin-β2==
<Structure load='4OO6' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (<scene name='37/372730/2h4m_cadetblue_centerspinpt3/1'>Kap-β2</scene>) is an importin that transports various cargo proteininto the nucleus through interactions with nucleoporins, which are proteins of the nuclear pore complex (NPC). The NPC is a large structure consisting of 456 constituent binding proteins called [https://en.wikipedia.org/wiki/Nucleoporin nucleoporins] (Nups). 1 Movement through the NPC is facilitated transport that relies on interaction with specific Nups. Importins and exportins are proteins that aid this facilitated transport by both binding to a specific cargo to be transported and interacting with specific Nups located in the central channel of the NPC.2 One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport ofRNA- binding proteins involved in transcription, RNA processing, RNA transportand translation. The structure of KAPβ is composed of 20 antiparallel helicescalled HEAT repeats. These HEAT repeats contribute to kapβ2’s largesuperhelical shape. That form two arches: one at the N-terminal and the other at the C- terminal. Through recognition of a [https://en.wikipedia.org/wiki/Nuclear_localization_sequence Nuclear Localization Signal] located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

The 3D structure of the Kapβ2, highlighed in cornflowerblue, shows one of the 20 [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats] in silver <scene name='37/372730/4oo6_heatrep_hr3/2'>HR3</scene>.

The NLS located on Kapβ2 cargos are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The electrostatic potential of the internal surface of Kapβ2 superhelix at the C-terminal arch is negative.
Recognition of the PY-NLS by Kapβ2 fallows certain guidelines:
(i)PY-NLS, when not bound to Kapβ2, lacks secondary structures.
(ii)PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2.
(iii)General sequence for the PY-NLS is either a hydrophobic or basic motif at the N-terminus and a R-X P-Y motif at the C-terminus.

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<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. The recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

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<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. the recognition of the <scene name='37/372748/Kapb2_rainbow_nls/1'>PY-NLS</scene> by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

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<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. the recognition of the PY-NLS by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5P-Y motif at the C-terminus.

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<StructureSection load= size=475 side='right' scene='37/372748/Kapb2_rainbow/1'>

== Karyopharin Beta 2 ==

Karyopherinβ is a group of proteins that is composed of both importins and exportins. Importins are proteins that carry cargos into the nucleus while exportins serve the opposite function. As of today, twenty different Kapβs have been identified. Each of these Kapβs is capable of recognizing and transporting a specific group of cargos. In order to bind to its cargo a Kapβ has to recognize a Nuclear Localization or Export Signal (NLS or NES).

Karyopherin beta 2 (kapβ2) is an importin that transports various cargo protein into the nucleus through interactions with nucleoporins, which are proteins of the nucleopore complex (NPC). One might overlook the significance of this protein but actually plays a crucial role in the human body by mediating transport of RNA- binding proteins involved in transcription, RNA processing, RNA transport and translation. The structure of KAPβ is composed of 20 antiparallel helices called [https://en.wikipedia.org/wiki/HEAT_repeat_domain HEAT repeats]. These <scene name='37/372748/Kapb2_rainbow_heat/2'>HEAT</scene> repeats contribute to kapβ2’s large <scene name='37/372748/Kapb2_rainbow_superhelical/1'>superhelical shape</scene>. That form two arches: one at the <scene name='37/372748/Kapb2_rainbow_nterminal/1'>N-terminal</scene> and the other at the <scene name='37/372748/Kapb2_rainbow_cterminal/1'>C-terminal</scene>. Through recognition of a nuclear localization signal (NLS) located on its cargo, kapβ2 binds to its cargo via its C-terminal arch. Release of the cargo is mediated by RanGTP, which once bound, modifies the shape of kapβ2. Release of the cargo is mediated once contact occurs between RanGTP and N-terminal arch of Kapβ2.

== How does Kapβ2 identify its cargo? ==

The NLS located on Kapβ2 cargos, are named the PY-NLS and they bind to the C-terminal arch of Kapβ2. The internal surface of kapβ2 superhelix at the C-terminal arch has negative electrostatic potential. the recognition of the PY-NLS by Kapβ2 follows certain guidelines: (1) PY-NLS, when not bound to Kapβ2, lacks a secondary structure; (2) PY-NLS has an overall positive charge allowing for electrostatic compatibility with Kapβ2; (3) the general sequence for PY-NLS is either a hydrophobic or a basic motif at the N-terminus and a R-X2-5

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