2ihs: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE= gus ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
|GENE= gus ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
|DOMAIN=
|RELATEDENTRY=[[2fnj|2FNJ]], [[2fbe|2FBE]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ihs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihs OCA], [http://www.ebi.ac.uk/pdbsum/2ihs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ihs RCSB]</span>
}}
}}


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[[Category: vasa]]
[[Category: vasa]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:29:44 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:44:31 2008''

Revision as of 03:44, 31 March 2008

File:2ihs.jpg


PDB ID 2ihs

Drag the structure with the mouse to rotate
, resolution 2.2Å
Gene: gus (Drosophila melanogaster)
Related: 2FNJ, 2FBE


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide


OverviewOverview

B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.

About this StructureAbout this Structure

2IHS is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for protein recognition by B30.2/SPRY domains., Woo JS, Suh HY, Park SY, Oh BH, Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197

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