2iui: Difference between revisions

New page: left|200px<br /> <applet load="2iui" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iui, resolution 2.40Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:2iui.gif|left|200px]]<br />
[[Image:2iui.gif|left|200px]]<br /><applet load="2iui" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2iui" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2iui, resolution 2.40&Aring;" />
caption="2iui, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE'''<br />
'''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE'''<br />


==Overview==
==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.
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==
2IUI 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IUI OCA].  
2IUI 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=2IUI OCA].  


==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Eck, M.J.]]
[[Category: Eck, M J.]]
[[Category: Harrison, S.C.]]
[[Category: Harrison, S C.]]
[[Category: Nolte, R.T.]]
[[Category: Nolte, R T.]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger, J.]]
[[Category: Shoelson, S.E.]]
[[Category: Shoelson, S E.]]
[[Category: disease mutation]]
[[Category: disease mutation]]
[[Category: p85]]
[[Category: p85]]
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[[Category: ubl conjugation]]
[[Category: ubl conjugation]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:06 2008''

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