From Proteopedia
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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= }} |
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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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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10601011}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10601011 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10601011}} |
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| | ==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
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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