1by2: Difference between revisions
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<StructureSection load='1by2' size='340' side='right'caption='[[1by2]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1by2' size='340' side='right'caption='[[1by2]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1by2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1by2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BY2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1by2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by2 OCA], [https://pdbe.org/1by2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1by2 RCSB], [https://www.ebi.ac.uk/pdbsum/1by2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1by2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/LG3BP_HUMAN LG3BP_HUMAN]] Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells.<ref>PMID:8034587</ref> <ref>PMID:11146440</ref> <ref>PMID:9501082</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 13:41, 19 May 2021
STRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAINSTRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN
Structural highlights
Function[LG3BP_HUMAN] Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells.[1] [2] [3] 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 found widely in cell surface molecules and in some secreted proteins, where they are thought to mediate ligand binding. We have determined the crystal structure at 2.0 A resolution of the SRCR domain of Mac-2 binding protein (M2BP), a tumor-associated antigen and matrix protein. The structure reveals a curved six-stranded beta-sheet cradling an alpha-helix. Structure-based sequence alignment demonstrates that the M2BP SRCR domain is a valid template for the entire SRCR protein superfamily. This allows an interpretation of previous mutagenesis data on ligand binding to the lymphocyte receptor CD6. Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily.,Hohenester E, Sasaki T, Timpl R Nat Struct Biol. 1999 Mar;6(3):228-32. PMID:10074941[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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