2iug: Difference between revisions
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[[Image:2iug.gif|left|200px]] | [[Image:2iug.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN''' | {{Structure | ||
|PDB= 2iug |SIZE=350|CAPTION= <scene name='initialview01'>2iug</scene>, resolution 1.89Å | |||
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'''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2IUG is a [ | 2IUG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8599763 8599763] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubl conjugation]] | [[Category: ubl conjugation]] | ||
''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 17:33:29 2008'' |
Revision as of 18:33, 20 March 2008
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, resolution 1.89Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN
OverviewOverview
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 StructureAbout this Structure
2IUG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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