1sps: Difference between revisions
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[[Image:1sps.gif|left|200px]] | [[Image:1sps.gif|left|200px]] | ||
'''BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS''' | {{Structure | ||
|PDB= 1sps |SIZE=350|CAPTION= <scene name='initialview01'>1sps</scene>, resolution 2.7Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO3:PHOSPHITE ION'>PO3</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SPS is a [ | 1SPS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Hamster_polyomavirus Hamster polyomavirus] and [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPS OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7680960 7680960] | ||
[[Category: Hamster polyomavirus]] | [[Category: Hamster polyomavirus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:06 2008'' | ||
Revision as of 15:08, 20 March 2008
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BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS
OverviewOverview
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 StructureAbout this Structure
1SPS is a Protein complex structure of sequences from Hamster polyomavirus and Rous sarcoma virus. Full crystallographic information is available from OCA.
ReferenceReference
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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