3eaz: Difference between revisions

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 ==Crystal structure of SH2 domain of Human Csk (carboxyl-terminal src kinase), C122S mutant.==
-<StructureSection load='3eaz' size='340' side='right' caption='[[3eaz]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
+<StructureSection load='3eaz' size='340' side='right'caption='[[3eaz]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3eaz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EAZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3eaz]] is a 1 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=3EAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EAZ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eac|3eac]], [[1k9a|1k9a]]</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]] 1.31&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3eaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eaz OCA], [https://pdbe.org/3eaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eaz RCSB], [https://www.ebi.ac.uk/pdbsum/3eaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eaz ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span></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=3eaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eaz OCA], [http://pdbe.org/3eaz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eaz RCSB], [http://www.ebi.ac.uk/pdbsum/3eaz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eaz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CSK_HUMAN CSK_HUMAN]] 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.<ref>PMID:1639064</ref> <ref>PMID:9281320</ref>
+[https://www.uniprot.org/uniprot/CSK_HUMAN CSK_HUMAN] 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.<ref>PMID:1639064</ref> <ref>PMID:9281320</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 30: @@
 ==See Also==
-*[[Tyrosine kinase|Tyrosine kinase]]
+*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Non-specific protein-tyrosine kinase]]
+[[Category: Large Structures]]
-[[Category: Cowburn, D]]
+[[Category: Cowburn D]]
-[[Category: Liu, D]]
+[[Category: Liu D]]
-[[Category: Seidel, R D]]
+[[Category: Seidel RD]]
-[[Category: Atp-binding]]
-[[Category: Cell membrane]]
-[[Category: Csk]]
-[[Category: Disulfide]]
-[[Category: Kinase]]
-[[Category: Membrane]]
-[[Category: Nucleotide-binding]]
-[[Category: Oxidized reduced]]
-[[Category: Phosphoprotein]]
-[[Category: Sh2]]
-[[Category: Sh2 domain]]
-[[Category: Sh3 domain]]
-[[Category: Transferase]]
-[[Category: Tyrosine-protein kinase]]