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[[Image:1dcq.gif|left|200px]]
{{Seed}}
[[Image:1dcq.png|left|200px]]


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{{STRUCTURE_1dcq|  PDB=1dcq  |  SCENE=  }}  
{{STRUCTURE_1dcq|  PDB=1dcq  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.'''
===CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.===




==Overview==
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ADP ribosylation factors (ARFs), which are members of the Ras superfamily of GTP-binding proteins, are critical components of vesicular trafficking pathways in eukaryotes. Like Ras, ARFs are active in their GTP-bound form, and their duration of activity is controlled by GTPase-activating proteins (GAPs), which assist ARFs in hydrolyzing GTP to GDP. PAPbeta, a protein that binds to and is phosphorylated by the non-receptor tyrosine kinase PYK2, contains several modular signaling domains including a pleckstrin homology domain, an SH3 domain, ankyrin repeats and an ARF-GAP domain. Sequences of ARF-GAP domains show no recognizable similarity to those of other GAPs, and contain a characteristic Cys-X(2)-Cys-X(16-17)-Cys-X(2)-Cys motif. The crystal structure of the PAPbeta ARF-GAP domain and the C-terminal ankyrin repeats has been determined at 2.1 A resolution. The ARF-GAP domain comprises a central three-stranded beta-sheet flanked by five alpha-helices, with a Zn(2+) ion coordinated by the four cysteines of the cysteine-rich motif. Four ankyrin repeats are also present, the first two of which form an extensive interface with the ARF-GAP domain. An invariant arginine and several nearby hydrophobic residues are solvent exposed and are predicted to be the site of interaction with ARFs. Site-directed mutagenesis of these residues confirms their importance in ARF-GAP activity.
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{{ABSTRACT_PUBMED_10601011}}


==About this Structure==
==About this Structure==
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[[Category: Ankyrin repeat]]
[[Category: Ankyrin repeat]]
[[Category: Zinc-binding module]]
[[Category: Zinc-binding module]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:42:03 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:49:54 2008''

Revision as of 19:49, 30 June 2008

File:1dcq.png

Template:STRUCTURE 1dcq

CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.

Template:ABSTRACT PUBMED 10601011

About this Structure

1DCQ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta., Mandiyan V, Andreev J, Schlessinger J, Hubbard SR, EMBO J. 1999 Dec 15;18(24):6890-8. PMID:10601011

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