2ja4: Difference between revisions
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<StructureSection load='2ja4' size='340' side='right'caption='[[2ja4]], [[Resolution|resolution]] 2.21Å' scene=''> | <StructureSection load='2ja4' size='340' side='right'caption='[[2ja4]], [[Resolution|resolution]] 2.21Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ja4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JA4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[2ja4]] 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=2JA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JA4 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</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=2ja4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ja4 OCA], [https://pdbe.org/2ja4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ja4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ja4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ja4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CD5_HUMAN CD5_HUMAN] May act as a receptor in regulating T-cell proliferation. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/2ja4_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/2ja4_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Blanco | [[Category: Blanco FJ]] | ||
[[Category: Lozano | [[Category: Lozano F]] | ||
[[Category: Montoya | [[Category: Montoya G]] | ||
[[Category: Munoz | [[Category: Munoz IG]] | ||
[[Category: Rodamilans | [[Category: Rodamilans B]] | ||
[[Category: Sarrias | [[Category: Sarrias MR]] | ||
Latest revision as of 08:18, 17 October 2024
Crystal structure of CD5 domain III reveals the fold of a group B scavenger cysteine-rich receptorCrystal structure of CD5 domain III reveals the fold of a group B scavenger cysteine-rich receptor
Structural highlights
FunctionCD5_HUMAN May act as a receptor in regulating T-cell proliferation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedScavenger receptor cysteine-rich (SRCR) domains are ancient protein modules widely found among cell surface and secreted proteins of the innate and adaptive immune system, where they mediate ligand binding. We have solved the crystal structure at 2.2 A of resolution of the SRCR CD5 domain III, a human lymphocyte receptor involved in the modulation of antigen specific receptor-mediated T cell activation and differentiation signals. The first structure of a member of a group B SRCR domain reveals the fold of this ancient protein module into a central core formed by two antiparallel beta-sheets and one alpha-helix, illustrating the conserved core at the protein level of genes coding for group A and B members of the SRCR superfamily. The novel SRCR group B structure permits the interpretation of site-directed mutagenesis data on the binding of activated leukocyte cell adhesion molecule (ALCAM/CD166) binding to CD6, a closely related lymphocyte receptor homologue to CD5. Crystal structure of the third extracellular domain of CD5 reveals the fold of a group B scavenger cysteine-rich receptor domain.,Rodamilans B, Munoz IG, Bragado-Nilsson E, Sarrias MR, Padilla O, Blanco FJ, Lozano F, Montoya G J Biol Chem. 2007 Apr 27;282(17):12669-77. Epub 2007 Feb 23. PMID:17322294[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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