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==Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP==
==Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP==
<StructureSection load='1jeg' size='340' side='right'caption='[[1jeg]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
<StructureSection load='1jeg' size='340' side='right'caption='[[1jeg]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jeg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JEG FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jeg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JEG 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/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </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=1jeg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeg OCA], [http://pdbe.org/1jeg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jeg RCSB], [http://www.ebi.ac.uk/pdbsum/1jeg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jeg 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=1jeg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeg OCA], [https://pdbe.org/1jeg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jeg RCSB], [https://www.ebi.ac.uk/pdbsum/1jeg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jeg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CSK_MOUSE CSK_MOUSE]] Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity). [[http://www.uniprot.org/uniprot/PTN22_MOUSE PTN22_MOUSE]] Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-492' residue. Dephosphorylates the immune system activator SKAP2 (By similarity).<ref>PMID:8890164</ref>
[https://www.uniprot.org/uniprot/PTN22_MOUSE PTN22_MOUSE] Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-492' residue. Dephosphorylates the immune system activator SKAP2 (By similarity).<ref>PMID:8890164</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Tyrosine kinase|Tyrosine kinase]]
*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Transferase]]
[[Category: Cowburn D]]
[[Category: Cowburn, D]]
[[Category: Ghose R]]
[[Category: Ghose, R]]
[[Category: Goger MJ]]
[[Category: Goger, M J]]
[[Category: Ji H]]
[[Category: Ji, H]]
[[Category: Shekhtman A]]
[[Category: Shekhtman, A]]
[[Category: Kinase]]
[[Category: Protein-peptide complex]]
[[Category: Sh3 domain]]
[[Category: Transferase-hydrolase complex]]
[[Category: Tyrosine phosphatase]]
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