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1pkt

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Revision as of 06:51, 29 November 2017

STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY

Structural highlights

1pkt is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1pks
Activity:	Phosphatidylinositol 3-kinase, with EC number 2.7.1.137
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Src homology 3 (SH3) domains, which are found in many proteins involved in intracellular signal transduction, mediate specific protein-protein interactions. The three-dimensional structure of the SH3 domain in the p85 subunit of the phosphatidylinositol 3-kinase (PI3K) has been determined by multidimensional NMR methods. The molecule consists of four short helices, two beta turns, and two antiparallel beta sheets. The beta sheets are highly similar to corresponding regions in the SH3 domain of the tyrosine kinase Src, even though the sequence identity of the two domains is low. There is a unique 15 amino acid insert in PI3K that contains three short helices. There are substantial differences in the identity of the amino acids that make up the receptor site of SH3 domains. The results suggest that while the overall structures of the binding sites in the PI3K and Src SH3 domains are similar, their ligand binding properties may differ.

Structure of the PI3K SH3 domain and analysis of the SH3 family.,Koyama S, Yu H, Dalgarno DC, Shin TB, Zydowsky LD, Schreiber SL Cell. 1993 Mar 26;72(6):945-52. PMID:7681364^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vainikka S, Joukov V, Wennstrom S, Bergman M, Pelicci PG, Alitalo K. Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1. J Biol Chem. 1994 Jul 15;269(28):18320-6. PMID:7518429
↑ Miled N, Yan Y, Hon WC, Perisic O, Zvelebil M, Inbar Y, Schneidman-Duhovny D, Wolfson HJ, Backer JM, Williams RL. Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit. Science. 2007 Jul 13;317(5835):239-42. PMID:17626883 doi:317/5835/239
↑ Mandelker D, Gabelli SB, Schmidt-Kittler O, Zhu J, Cheong I, Huang CH, Kinzler KW, Vogelstein B, Amzel LM. A frequent kinase domain mutation that changes the interaction between PI3Kalpha and the membrane. Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):16996-7001. Epub 2009 Sep 23. PMID:19805105
↑ Koyama S, Yu H, Dalgarno DC, Shin TB, Zydowsky LD, Schreiber SL. Structure of the PI3K SH3 domain and analysis of the SH3 family. Cell. 1993 Mar 26;72(6):945-52. PMID:7681364

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pkt"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY==
 <StructureSection load='1pkt' size='340' side='right' caption='[[1pkt]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pks|1pks]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_3-kinase Phosphatidylinositol 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.137 2.7.1.137] </span></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=1pkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkt OCA], [http://pdbe.org/1pkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pkt RCSB], [http://www.ebi.ac.uk/pdbsum/1pkt PDBsum]</span></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=1pkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pkt OCA], [http://pdbe.org/1pkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pkt RCSB], [http://www.ebi.ac.uk/pdbsum/1pkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pkt ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1pkt" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Phosphoinositide 3-Kinases|Phosphoinositide 3-Kinases]]
 == References ==
 <references/>

1pkt

From Proteopedia

Revision as of 06:51, 29 November 2017

STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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