1dcq

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcq OCA], [http://www.ebi.ac.uk/pdbsum/1dcq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dcq RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.'''
'''CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.'''
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[[Category: Mandiyan, V.]]
[[Category: Mandiyan, V.]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger, J.]]
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[[Category: ankyrin repeat]]
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[[Category: Ankyrin repeat]]
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[[Category: zinc-binding module]]
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[[Category: Zinc-binding module]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:42:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:07 2008''
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Revision as of 10:42, 2 May 2008

Template:STRUCTURE 1dcq

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


Overview

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.

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 Page seeded by OCA on Fri May 2 13:42:03 2008

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