1stp: Difference between revisions

Line 1:

[[Image:1stp.gif|left|200px]]<br /><applet load="1stp" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1stp.gif|left|200px]]<br /><applet load="1stp" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1stp, resolution 2.6Å" />

'''STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN'''<br />

==Overview==

The high affinity of the noncovalent interaction between biotin and, streptavidin forms the basis for many diagnostic assays that require the, formation of an irreversible and specific linkage between biological, macromolecules. Comparison of the refined crystal structures of apo and a, streptavidin:biotin complex shows that the high affinity results from, several factors. These factors include the formation of multiple hydrogen, bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the, biotin in the protein interior. Structural alterations at the biotin, binding site produce quaternary changes in the streptavidin tetramer., These changes apparently propagate through cooperative deformations in the, twisted beta sheets that link tetramer subunits.

The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.

==About this Structure==

1STP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with BTN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1STP OCA].

1STP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with <scene name='pdbligand=BTN:'>BTN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STP OCA].

==Reference==

Line 13:

[[Category: Single protein]]

[[Category: Streptomyces avidinii]]

[[Category: Salemme, F.R.]]

[[Category: Salemme, F R.]]

[[Category: Weber, P.C.]]

[[Category: Weber, P C.]]

[[Category: BTN]]

[[Category: biotin binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:39:~~29 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:03 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1stp.gif|left|200px]]<br /><applet load="1stp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1stp.gif|left|200px]]<br /><applet load="1stp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1stp, resolution 2.6&Aring;" />
 '''STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN'''<br />
 ==Overview==
-The high affinity of the noncovalent interaction between biotin and, streptavidin forms the basis for many diagnostic assays that require the, formation of an irreversible and specific linkage between biological, macromolecules. Comparison of the refined crystal structures of apo and a, streptavidin:biotin complex shows that the high affinity results from, several factors. These factors include the formation of multiple hydrogen, bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the, biotin in the protein interior. Structural alterations at the biotin, binding site produce quaternary changes in the streptavidin tetramer., These changes apparently propagate through cooperative deformations in the, twisted beta sheets that link tetramer subunits.
+The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.
 ==About this Structure==
-STP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with BTN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1STP OCA].
+STP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with <scene name='pdbligand=BTN:'>BTN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STP OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Streptomyces avidinii]]
-[[Category: Salemme, F.R.]]
+[[Category: Salemme, F R.]]
-[[Category: Weber, P.C.]]
+[[Category: Weber, P C.]]
 [[Category: BTN]]
 [[Category: biotin binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:39:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:03 2008''