1nwm

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{{STRUCTURE_1nwm| PDB=1nwm | SCENE= }}
{{STRUCTURE_1nwm| PDB=1nwm | SCENE= }}
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'''GAT domain of human GGA1'''
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===GAT domain of human GGA1===
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==Overview==
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The Golgi-associated, gamma-adaptin homologous, ADP-ribosylation factor (ARF)-interacting proteins (GGAs) are adaptors that sort receptors from the trans-Golgi network into the endosomallysosomal pathway. The GGAs and TOM1 (GAT) domains of the GGAs are responsible for their ARF-dependent localization. The 2.4-A crystal structure of the GAT domain of human GGA1 reveals a three-helix bundle, with a long N-terminal helical extension that is not conserved in GAT domains that do not bind ARF. The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle. An unanticipated structural similarity to the N-terminal domain of syntaxin 1a was discovered, comprising the entire three-helix bundle. A conserved binding site on helices 2 and 3 of the GAT domain three-helix bundle is predicted to interact with coiled-coil-containing proteins. We propose that the GAT domain is descended from the same ancestor as the syntaxin 1a N-terminal domain, and that both protein families share a common function in binding coiled-coil domain proteins.
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{{ABSTRACT_PUBMED_12668765}}
==About this Structure==
==About this Structure==
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[[Category: Suer, S.]]
[[Category: Suer, S.]]
[[Category: Three-alpha helical bundle]]
[[Category: Three-alpha helical bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:04:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:56:11 2008''

Revision as of 08:56, 29 July 2008

Template:STRUCTURE 1nwm

GAT domain of human GGA1

Template:ABSTRACT PUBMED 12668765

About this Structure

1NWM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor., Suer S, Misra S, Saidi LF, Hurley JH, Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4451-6. Epub 2003 Mar 31. PMID:12668765

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