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2iui
From Proteopedia
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE
Overview
Crystal structures of the amino-terminal SH2 domain of the p85alpha subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that phosphopeptides bind in the two-pronged manner seen in high-affinity Lck and Src SH2 complexes, with conserved interactions between the domain and the peptide segment from phosphotyrosine to Met+3. Peptide binding requires the rearrangement of a tyrosyl side chain in the BG loop to create the hydrophobic Met+3 binding pocket. The structures suggest a mechanism for the biological specificity exhibited by PI 3-kinase in its interactions with phosphoprotein partners.
About this Structure
2IUI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes., Nolte RT, Eck MJ, Schlessinger J, Shoelson SE, Harrison SC, Nat Struct Biol. 1996 Apr;3(4):364-74. PMID:8599763
Page seeded by OCA on Mon Mar 31 03:48:48 2008
Categories: Homo sapiens | Single protein | Eck, M J. | Harrison, S C. | Nolte, R T. | Schlessinger, J. | Shoelson, S E. | Disease mutation | P85 | Phosphorylation | Pi3-kinase | Pi3k | Polymorphism | Sh2 | Sh2 domain | Sh3 domain | Transferase | Ubl conjugation
