2iug: Difference between revisions
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==Crystal structure of the PI3-kinase p85 N-terminal SH2 domain== | ==Crystal structure of the PI3-kinase p85 N-terminal SH2 domain== | ||
<StructureSection load='2iug' size='340' side='right' caption='[[2iug]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='2iug' size='340' side='right'caption='[[2iug]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2iug]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUG OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2iug]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IUG FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a0n|1a0n]], [[1azg|1azg]], [[1h9o|1h9o]], [[1pbw|1pbw]], [[1pht|1pht]], [[1pic|1pic]], [[1pks|1pks]], [[1pkt|1pkt]], [[2iuh|2iuh]], [[2iui|2iui]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a0n|1a0n]], [[1azg|1azg]], [[1h9o|1h9o]], [[1pbw|1pbw]], [[1pht|1pht]], [[1pic|1pic]], [[1pks|1pks]], [[1pkt|1pkt]], [[2iuh|2iuh]], [[2iui|2iui]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2iug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iug OCA], [http://pdbe.org/2iug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iug RCSB], [http://www.ebi.ac.uk/pdbsum/2iug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iug ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Phosphoinositide 3- | *[[Phosphoinositide 3-kinase 3D structures|Phosphoinositide 3-kinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Eck, M J]] | [[Category: Eck, M J]] | ||
[[Category: Harrison, S C]] | [[Category: Harrison, S C]] | ||
Revision as of 10:51, 8 April 2020
Crystal structure of the PI3-kinase p85 N-terminal SH2 domainCrystal structure of the PI3-kinase p85 N-terminal SH2 domain
Structural highlights
Function[P85A_HUMAN] Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal 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 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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