5o2p: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 ==p130Cas SH3 domain PTP-PEST peptide chimera==
-<StructureSection load='5o2p' size='340' side='right' caption='[[5o2p]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
+<StructureSection load='5o2p' size='340' side='right'caption='[[5o2p]]' scene=''>
 == 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O2P FirstGlance]. <br>
+<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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5o2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o2p OCA], [http://pdbe.org/5o2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o2p RCSB], [http://www.ebi.ac.uk/pdbsum/5o2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o2p 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=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>
+== 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;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 </div>
 <div class="pdbe-citations 5o2p" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Homo sapiens]]
-[[Category: Hexnerova, R]]
+[[Category: Large Structures]]
-[[Category: Veverka, V]]
+[[Category: Hexnerova R]]
-[[Category: P130ca]]
+[[Category: Veverka V]]
-[[Category: Sh3 domain]]
-[[Category: Structure from cyana 3 97]]