4ey0: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ey0]] is a 4 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=4EY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EY0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ey0]] is a 4 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=4EY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EY0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></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]] 2.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></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=4ey0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey0 OCA], [https://pdbe.org/4ey0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ey0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ey0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey0 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=4ey0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey0 OCA], [https://pdbe.org/4ey0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ey0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ey0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 05:51, 21 November 2024
Structure of tandem SH2 domains from PLCgamma1Structure of tandem SH2 domains from PLCgamma1
Structural highlights
Publication Abstract from PubMedMultidomain proteins incorporating interaction domains are central to regulation of cellular processes. The elucidation of structural organization and mechanistic insights into many of these proteins, however, remain challenging due to their inherent flexibility. Here, we describe the organization and function of four interaction domains in PLCgamma1 using a combination of structural biology and biochemical approaches. Intramolecular interactions within the regulatory region center on the cSH2 domain, the only domain that also interacts with the PLC-core. In the context of fibroblast growth-factor receptor signaling, the coordinated involvement of nSH2 and cSH2 domains mediates efficient phosphorylation of PLCgamma1 resulting in the interruption of an autoinhibitory interface by direct competition and, independently, dissociation of PLCgamma1 from the receptor. Further structural insights into the autoinhibitory surfaces provide a framework to interpret gain-of-function mutations in PLCgamma isoforms linked to immune disorders and illustrate a distinct mechanism for regulation of PLC activity by common interaction domains. Structural and functional integration of the PLCgamma interaction domains critical for regulatory mechanisms and signaling deregulation.,Bunney TD, Esposito D, Mas-Droux C, Lamber E, Baxendale RW, Martins M, Cole A, Svergun D, Driscoll PC, Katan M Structure. 2012 Dec 5;20(12):2062-75. doi: 10.1016/j.str.2012.09.005. Epub 2012, Oct 11. PMID:23063561[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||