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| | ==Crystal structure of iSH2 domain of human p85beta, Northeast Structural Genomics Consortium Target HR5531C== | | ==Crystal structure of iSH2 domain of human p85beta, Northeast Structural Genomics Consortium Target HR5531C== |
| - | <StructureSection load='3mtt' size='340' side='right' caption='[[3mtt]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <StructureSection load='3mtt' size='340' side='right'caption='[[3mtt]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mtt]] 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=3MTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MTT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mtt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MTT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIK3R2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtt OCA], [http://pdbe.org/3mtt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mtt RCSB], [http://www.ebi.ac.uk/pdbsum/3mtt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtt ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtt OCA], [https://pdbe.org/3mtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mtt RCSB], [https://www.ebi.ac.uk/pdbsum/3mtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/P85B_HUMAN P85B_HUMAN]] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. | + | [https://www.uniprot.org/uniprot/P85B_HUMAN P85B_HUMAN] Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphoinositide 3-Kinases|Phosphoinositide 3-Kinases]] | + | *[[Phosphoinositide 3-kinase 3D structures|Phosphoinositide 3-kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Guan, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Krug, R M]] | + | [[Category: Guan R]] |
| - | [[Category: Ma, L C]] | + | [[Category: Krug RM]] |
| - | [[Category: Montelione, G T]] | + | [[Category: Ma LC]] |
| - | [[Category: Structural genomic]] | + | [[Category: Montelione GT]] |
| - | [[Category: Schauder, C]] | + | [[Category: Schauder C]] |
| - | [[Category: Inter-sh2 domain]]
| + | |
| - | [[Category: Nesg]]
| + | |
| - | [[Category: Pi3-kinase subunit p85-beta]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
P85B_HUMAN Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane.
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 PubMed
Phosphatidylinositol 3-kinase (PI3K) proteins actively trigger signaling pathways leading to cell growth, proliferation and survival. These proteins have multiple isoforms and consist of a catalytic p110 subunit and a regulatory p85 subunit. The iSH2 domain of the p85beta isoform has been implicated in the binding of nonstructural protein 1 (NS1) of influenza A viruses. Here, the crystal structure of human p85beta iSH2 determined to 3.3 A resolution is reported. The structure reveals that this domain mainly consists of a coiled-coil motif. Comparison with the published structure of the bovine p85beta iSH2 domain bound to the influenza A virus nonstructural protein 1 indicates that little or no structural change occurs upon complex formation. By comparing this human p85beta iSH2 structure with the bovine p85beta iSH2 domain, which shares 99% sequence identity, and by comparing the multiple conformations observed within the asymmetric unit of the bovine iSH2 structure, it was found that this coiled-coil domain exhibits a certain degree of conformational variability or `plasticity' in the interhelical turn region. It is speculated that this plasticity of p85beta iSH2 may play a role in regulating its functional and molecular-recognition properties.
Structure of the iSH2 domain of human phosphatidylinositol 3-kinase p85beta subunit reveals conformational plasticity in the interhelical turn region.,Schauder C, Ma LC, Krug RM, Montelione GT, Guan R Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1567-71. Epub 2010 Nov 16. PMID:21139197[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schauder C, Ma LC, Krug RM, Montelione GT, Guan R. Structure of the iSH2 domain of human phosphatidylinositol 3-kinase p85beta subunit reveals conformational plasticity in the interhelical turn region. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1567-71. Epub 2010 Nov 16. PMID:21139197 doi:10.1107/S1744309110041333
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