2jcr: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /> <applet load="2jcr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jcr, resolution 2.00Å" /> '''THE HYALURONAN BIND... |
No edit summary |
||
| (22 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==The hyaluronan binding domain of murine CD44 in a Type B complex with an HA 8-mer== | ||
<StructureSection load='2jcr' size='340' side='right'caption='[[2jcr]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jcr]] 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=2JCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JCR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=2jcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jcr OCA], [https://pdbe.org/2jcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jcr RCSB], [https://www.ebi.ac.uk/pdbsum/2jcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jcr ProSAT]</span></td></tr> | |||
</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 == | |||
[[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/jc/2jcr_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2jcr ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Regulation 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<ref>PMID:17293874</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jcr" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CD44|CD44]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Banerji S]] | |||
[[Category: Banerji | [[Category: Campbell ID]] | ||
[[Category: Campbell | [[Category: Day AJ]] | ||
[[Category: Day | [[Category: Jackson DG]] | ||
[[Category: Jackson | [[Category: Mahoney DJ]] | ||
[[Category: Mahoney | [[Category: Noble MEM]] | ||
[[Category: Noble | [[Category: Wright AJ]] | ||
[[Category: Wright | |||
Latest revision as of 04:05, 21 November 2024
The hyaluronan binding domain of murine CD44 in a Type B complex with an HA 8-merThe hyaluronan binding domain of murine CD44 in a Type B complex with an HA 8-mer
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
|
| ||||||||||||||||||