2jcp: Difference between revisions
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<StructureSection load='2jcp' size='340' side='right'caption='[[2jcp]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='2jcp' size='340' side='right'caption='[[2jcp]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2jcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JCP FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</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=2jcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jcp OCA], [https://pdbe.org/2jcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jcp RCSB], [https://www.ebi.ac.uk/pdbsum/2jcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jcp 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=2jcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jcp OCA], [https://pdbe.org/2jcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jcp RCSB], [https://www.ebi.ac.uk/pdbsum/2jcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jcp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CD44_MOUSE CD44_MOUSE] Main cell surface receptor for hyaluronate. Adhesion to mucosal high endothelial venule and to types I and VI collagen. Probably involved in matrix adhesion, lymphocyte activation and lymph node homing. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Banerji | [[Category: Banerji S]] | ||
[[Category: Campbell | [[Category: Campbell ID]] | ||
[[Category: Day | [[Category: Day AJ]] | ||
[[Category: Jackson | [[Category: Jackson DG]] | ||
[[Category: Mahoney | [[Category: Mahoney DJ]] | ||
[[Category: Noble | [[Category: Noble MEM]] | ||
[[Category: Wright | [[Category: Wright AJ]] | ||
Revision as of 17:43, 13 December 2023
The hyaluronan binding domain of murine CD44The hyaluronan binding domain of murine CD44
Structural highlights
FunctionCD44_MOUSE Main cell surface receptor for hyaluronate. Adhesion to mucosal high endothelial venule and to types I and VI collagen. Probably involved in matrix adhesion, lymphocyte activation and lymph node homing. 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 PubMedRegulation of transient interactions between cells and the ubiquitous matrix glycosaminoglycan hyaluronan is crucial to such fundamental processes as embryonic development and leukocyte homing. Cd44, the primary cell surface receptor for hyaluronan, binds ligand via a lectin-like fold termed the Link module, but only after appropriate functional activation. The molecular details of the Cd44-hyaluronan interaction and hence the structural basis for this activation are unknown. Here we present the first crystal structure of Cd44 complexed with hyaluronan. This reveals that the interaction with hyaluronan is dominated by shape and hydrogen-bonding complementarity and identifies two conformational forms of the receptor that differ in orientation of a crucial hyaluronan-binding residue (Arg45, equivalent to Arg41 in human CD44). Measurements by NMR indicate that the conformational transition can be induced by hyaluronan binding, providing further insight into possible mechanisms for regulation of Cd44. Structures of the Cd44-hyaluronan complex provide insight into a fundamental carbohydrate-protein interaction.,Banerji S, Wright AJ, Noble M, Mahoney DJ, Campbell ID, Day AJ, Jackson DG Nat Struct Mol Biol. 2007 Mar;14(3):234-9. Epub 2007 Feb 11. PMID:17293874[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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