5o2p: Difference between revisions
New page: ==p130Cas SH3 domain PTP-PEST peptide chimera== <StructureSection load='5o2p' size='340' side='right' caption='5o2p, 40 NMR models' scene=''> == Structur... |
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==p130Cas SH3 domain PTP-PEST peptide chimera== | ==p130Cas SH3 domain PTP-PEST peptide chimera== | ||
<StructureSection load='5o2p' size='340' side='right' caption='[[5o2p | <StructureSection load='5o2p' size='340' side='right'caption='[[5o2p]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o2p]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O2P OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5o2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O2P FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5o2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o2p OCA], [https://pdbe.org/5o2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o2p RCSB], [https://www.ebi.ac.uk/pdbsum/5o2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o2p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</ref> [https://www.uniprot.org/uniprot/PTN12_HUMAN PTN12_HUMAN] Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2.<ref>PMID:17329398</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5o2p" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5o2p" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Hexnerova R]] | ||
[[Category: | [[Category: Veverka V]] | ||
Latest revision as of 09:03, 19 June 2024
p130Cas SH3 domain PTP-PEST peptide chimerap130Cas SH3 domain PTP-PEST peptide chimera
Structural highlights
FunctionBCAR1_HUMAN Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.[1] [2] PTN12_HUMAN Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2.[3] Publication Abstract from PubMedCAS is a docking protein downstream of the proto-oncogene Src with a role in invasion and metastasis of cancer cells. The CAS SH3 domain is indispensable for CAS-mediated signaling, but structural aspects of CAS SH3 ligand binding and regulation are not well understood. Here, we identified the consensus CAS SH3 binding motif and structurally characterized the CAS SH3 domain in complex with ligand. We revealed the requirement for an uncommon centrally localized lysine residue at position +2 of CAS SH3 ligands and two rather dissimilar optional anchoring residues, leucine and arginine, at position +5. We further expanded the knowledge of CAS SH3 ligand binding regulation by manipulating tyrosine 12 phosphorylation and confirmed the negative role of this phosphorylation on CAS SH3 ligand binding. Finally, by exploiting the newly identified binding requirements of the CAS SH3 domain, we predicted and experimentally verified two novel CAS SH3 binding partners, DOK7 and GLIS2. Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.,Gemperle J, Hexnerova R, Lepsik M, Tesina P, Dibus M, Novotny M, Brabek J, Veverka V, Rosel D Sci Rep. 2017 Aug 14;7(1):8057. doi: 10.1038/s41598-017-08303-4. PMID:28808245[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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