1g83: Difference between revisions

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-{{Seed}}
-[[Image:1g83.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF FYN SH3-SH2==
-The line below this paragraph, containing "STRUCTURE_1g83", creates the "Structure Box" on the page.
+<StructureSection load='1g83' size='340' side='right'caption='[[1g83]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1g83]] is a 2 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=1G83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G83 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=1g83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g83 OCA], [https://pdbe.org/1g83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g83 RCSB], [https://www.ebi.ac.uk/pdbsum/1g83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g83 ProSAT]</span></td></tr>
-{{STRUCTURE_1g83|  PDB=1g83  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FYN_HUMAN FYN_HUMAN] Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1.<ref>PMID:7822789</ref> <ref>PMID:7568038</ref> <ref>PMID:11005864</ref> <ref>PMID:11162638</ref> <ref>PMID:11536198</ref> <ref>PMID:12788081</ref> <ref>PMID:12640114</ref> <ref>PMID:14761972</ref> <ref>PMID:15557120</ref> <ref>PMID:14707117</ref> <ref>PMID:15536091</ref> <ref>PMID:16387660</ref> <ref>PMID:16841086</ref> <ref>PMID:17194753</ref> <ref>PMID:18056706</ref> <ref>PMID:18258597</ref> <ref>PMID:19179337</ref> <ref>PMID:19652227</ref> <ref>PMID:20100835</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g8/1g83_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g83 ConSurf].
+<div style="clear:both"></div>
-===CRYSTAL STRUCTURE OF FYN SH3-SH2===
+==See Also==
+*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_11278857}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 11278857 is the PubMed ID number.
+</StructureSection>
--->
-{{ABSTRACT_PUBMED_11278857}}
-==About this Structure==
-G83 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G83 OCA].
-==Reference==
-<ref group="xtra">PMID:11278857</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Transferase]]
+[[Category: Large Structures]]
-[[Category: Arold, S T.]]
+[[Category: Arold ST]]
-[[Category: Campbell, I D.]]
+[[Category: Campbell ID]]
-[[Category: Ladbury, J E.]]
+[[Category: Ladbury JE]]
-[[Category: Mulhern, T D.]]
+[[Category: Mulhern TD]]
-[[Category: Noble, M E.M.]]
+[[Category: Noble MEM]]
-[[Category: Ulmer, T S.]]
+[[Category: Ulmer TS]]
-[[Category: Werner, J M.]]
+[[Category: Werner JM]]
-[[Category: 3-10 helix]]
-[[Category: Alpha helix]]
-[[Category: Antiparallel beta sheet]]
-[[Category: Beta barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:59:48 2009''