<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2otx ConSurf].
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Revision as of 16:53, 7 February 2016
Crystal Structure of A N-terminal Fragment of SKAP-HOM Containing both the Helical Dimerization Domain and the PH Domain
2otx is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[SKAP2_MOUSE] May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.[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
PH domains, by binding to phosphoinositides, often serve as membrane-targeting modules. Using crystallographic, biochemical, and cell biological approaches, we have uncovered a mechanism that the integrin-signaling adaptor Skap-hom uses to mediate cytoskeletal interactions. Skap-hom is a homodimer containing an N-terminal four-helix bundle dimerization domain, against which its two PH domains pack in a conformation incompatible with phosphoinositide binding. The isolated PH domains bind PI[3,4,5]P(3), and mutations targeting the dimerization domain or the PH domain's PI[3,4,5]P(3)-binding pocket prevent Skap-hom localization to ruffles. Targeting is retained when the PH domain is deleted or by combined mutation of the PI[3,4,5]P(3)-binding pocket and the PH/dimerization domain interface. Thus, the dimerization and PH domain form a PI[3,4,5]P(3)-responsive molecular switch that controls Skap-hom function.
The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch.,Swanson KD, Tang Y, Ceccarelli DF, Poy F, Sliwa JP, Neel BG, Eck MJ Mol Cell. 2008 Nov 21;32(4):564-75. PMID:19026786[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Curtis DJ, Jane SM, Hilton DJ, Dougherty L, Bodine DM, Begley CG. Adaptor protein SKAP55R is associated with myeloid differentiation and growth arrest. Exp Hematol. 2000 Nov;28(11):1250-9. PMID:11063873
↑Bourette RP, Therier J, Mouchiroud G. Macrophage colony-stimulating factor receptor induces tyrosine phosphorylation of SKAP55R adaptor and its association with actin. Cell Signal. 2005 Aug;17(8):941-9. Epub 2005 Jan 20. PMID:15894167 doi:https://dx.doi.org/S0898-6568(04)00262-1
↑Togni M, Swanson KD, Reimann S, Kliche S, Pearce AC, Simeoni L, Reinhold D, Wienands J, Neel BG, Schraven B, Gerber A. Regulation of in vitro and in vivo immune functions by the cytosolic adaptor protein SKAP-HOM. Mol Cell Biol. 2005 Sep;25(18):8052-63. PMID:16135797 doi:https://dx.doi.org/25/18/8052
↑Swanson KD, Tang Y, Ceccarelli DF, Poy F, Sliwa JP, Neel BG, Eck MJ. The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch. Mol Cell. 2008 Nov 21;32(4):564-75. PMID:19026786 doi:10.1016/j.molcel.2008.09.022
