5aul: Difference between revisions

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'''Unreleased structure'''


The entry 5aul is ON HOLD  until Paper Publication
==PI3K p85 C-terminal SH2 domain/CD28-derived peptide complex==
 
<StructureSection load='5aul' size='340' side='right' caption='[[5aul]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
Authors: Inaba, S., Numoto, N., Morii, H., Ikura, T., Oda, M., Ito, N.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5aul]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AUL FirstGlance]. <br>
Description: PI3K p85 C-terminal SH2 domain/CD28-derived peptide complex
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wa4|3wa4]]</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=5aul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aul OCA], [http://pdbe.org/5aul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aul RCSB], [http://www.ebi.ac.uk/pdbsum/5aul PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/P85A_HUMAN 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.<ref>PMID:7518429</ref> <ref>PMID:17626883</ref> <ref>PMID:19805105</ref>  [[http://www.uniprot.org/uniprot/CD28_HUMAN CD28_HUMAN]] Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival.  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ikura, T]]
[[Category: Inaba, S]]
[[Category: Inaba, S]]
[[Category: Ito, N]]
[[Category: Morii, H]]
[[Category: Numoto, N]]
[[Category: Numoto, N]]
[[Category: Oda, M]]
[[Category: Oda, M]]
[[Category: Morii, H]]
[[Category: Antigen]]
[[Category: Ito, N]]
[[Category: Phosphopeptide]]
[[Category: Ikura, T]]
[[Category: Signaling protein]]

Revision as of 01:53, 2 June 2016

PI3K p85 C-terminal SH2 domain/CD28-derived peptide complexPI3K p85 C-terminal SH2 domain/CD28-derived peptide complex

Structural highlights

5aul is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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] [CD28_HUMAN] Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival.

References

  1. 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
  2. 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
  3. 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

5aul, resolution 1.10Å

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