1b9k: Difference between revisions

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[[Image:1b9k.gif|left|200px]]<br /><applet load="1b9k" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1b9k.gif|left|200px]]<br /><applet load="1b9k" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1b9k, resolution 1.90Å" />

'''ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2'''<br />

==Overview==

The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa, "appendage" domain, which is joined to the rest of the protein via a, flexible linker. The 1.9 A resolution crystal structure of this domain, reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is, shown to inhibit transferrin uptake, whereas mutants in which interactions, with its binding partners are abolished do not. DPF/W motifs present in, appendage domain-binding partners are shown to play a crucial role in, their interactions with the domain. A single site for binding multiple, ligands would allow for temporal and spatial regulation in the recruitment, of components of the endocytic machinery.

The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa "appendage" domain, which is joined to the rest of the protein via a flexible linker. The 1.9 A resolution crystal structure of this domain reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is shown to inhibit transferrin uptake, whereas mutants in which interactions with its binding partners are abolished do not. DPF/W motifs present in appendage domain-binding partners are shown to play a crucial role in their interactions with the domain. A single site for binding multiple ligands would allow for temporal and spatial regulation in the recruitment of components of the endocytic machinery.

==About this Structure==

1B9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1B9K OCA].

1B9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9K OCA].

==Reference==

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Evans, P.R.]]

[[Category: Evans, P R.]]

[[Category: Owen, D.J.]]

[[Category: Owen, D J.]]

[[Category: adaptor]]

[[Category: endocytosis]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:28:~~54 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:56 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1b9k.gif|left|200px]]<br /><applet load="1b9k" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b9k.gif|left|200px]]<br /><applet load="1b9k" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b9k, resolution 1.90&Aring;" />
 '''ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2'''<br />
 ==Overview==
-The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa, "appendage" domain, which is joined to the rest of the protein via a, flexible linker. The 1.9 A resolution crystal structure of this domain, reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is, shown to inhibit transferrin uptake, whereas mutants in which interactions, with its binding partners are abolished do not. DPF/W motifs present in, appendage domain-binding partners are shown to play a crucial role in, their interactions with the domain. A single site for binding multiple, ligands would allow for temporal and spatial regulation in the recruitment, of components of the endocytic machinery.
+The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa "appendage" domain, which is joined to the rest of the protein via a flexible linker. The 1.9 A resolution crystal structure of this domain reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is shown to inhibit transferrin uptake, whereas mutants in which interactions with its binding partners are abolished do not. DPF/W motifs present in appendage domain-binding partners are shown to play a crucial role in their interactions with the domain. A single site for binding multiple ligands would allow for temporal and spatial regulation in the recruitment of components of the endocytic machinery.
 ==About this Structure==
-B9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B9K OCA].
+B9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9K OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Evans, P.R.]]
+[[Category: Evans, P R.]]
-[[Category: Owen, D.J.]]
+[[Category: Owen, D J.]]
 [[Category: adaptor]]
 [[Category: endocytosis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:28:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:56 2008''