1spr
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1spr |SIZE=350|CAPTION= <scene name='initialview01'>1spr</scene>, resolution 2.5Å | |PDB= 1spr |SIZE=350|CAPTION= <scene name='initialview01'>1spr</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1spr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spr OCA], [http://www.ebi.ac.uk/pdbsum/1spr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1spr RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
[[Category: Waksman, G.]] | [[Category: Waksman, G.]] | ||
| - | [[Category: PO4]] | ||
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:19 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS
Overview
The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide has been determined at 2.7 A resolution by X-ray diffraction. The peptide binds in an extended conformation and makes primary interactions with the SH2 domain at six central residues: PQ(pY)EEI. The phosphotyrosine and the isoleucine are tightly bound by two well-defined pockets on the protein surface, resulting in a complex that resembles a two-pronged plug engaging a two-holed socket. The glutamate residues are in solvent-exposed environments in the vicinity of basic side chains of the SH2 domain, and the two N-terminal residues cap the phosphotyrosine-binding site. The crystal structure of Src SH2 in the absence of peptide has been determined at 2.5 A resolution, and comparison with the structure of the high affinity complex reveals only localized and relatively small changes.
About this Structure
1SPR is a Single protein structure of sequence from Rous sarcoma virus. Full crystallographic information is available from OCA.
Reference
Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms., Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J, Cell. 1993 Mar 12;72(5):779-90. PMID:7680960
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