2iuh
From Proteopedia
(New page: 200px<br /> <applet load="2iuh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iuh, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O...) |
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- | [[Image:2iuh.gif|left|200px]]<br /> | + | [[Image:2iuh.gif|left|200px]]<br /><applet load="2iuh" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="2iuh" size=" | + | |
caption="2iuh, resolution 2.00Å" /> | caption="2iuh, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH C-KIT PHOSPHOTYROSYL PEPTIDE'''<br /> | '''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH C-KIT PHOSPHOTYROSYL PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
- | Crystal structures of the amino-terminal SH2 domain of the p85alpha | + | 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== | ==About this Structure== | ||
- | 2IUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2IUH is a [http://en.wikipedia.org/wiki/Single_protein 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=2IUH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Eck, M | + | [[Category: Eck, M J.]] |
- | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
- | [[Category: Nolte, R | + | [[Category: Nolte, R T.]] |
[[Category: Schlessinger, J.]] | [[Category: Schlessinger, J.]] | ||
- | [[Category: Shoelson, S | + | [[Category: Shoelson, S E.]] |
[[Category: disease mutation]] | [[Category: disease mutation]] | ||
[[Category: p85]] | [[Category: p85]] | ||
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[[Category: ubl conjugation]] | [[Category: ubl conjugation]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:10 2008'' |
Revision as of 15:56, 21 February 2008
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CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH C-KIT 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
2IUH 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 Thu Feb 21 17:56:10 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