2jcr: Difference between revisions

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-[[Image:2jcr.gif|left|200px]]
-<!--
+==The hyaluronan binding domain of murine CD44 in a Type B complex with an HA 8-mer==
-The line below this paragraph, containing "STRUCTURE_2jcr", creates the "Structure Box" on the page.
+<StructureSection load='2jcr' size='340' side='right'caption='[[2jcr]], [[Resolution|resolution]] 2.00&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'>[[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>
-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&#8491;</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>
-{{STRUCTURE_2jcr|  PDB=2jcr  |  SCENE=  }}
+<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.
-'''THE HYALURONAN BINDING DOMAIN OF MURINE CD44 IN A TYPE B COMPLEX WITH AN HA 8-MER'''
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2jcr" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-JCR is a [[Single protein]] structure of sequence from [http://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].
+*[[CD44|CD44]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Banerji S]]
-[[Category: Banerji, S.]]
+[[Category: Campbell ID]]
-[[Category: Campbell, I D.]]
+[[Category: Day AJ]]
-[[Category: Day, A J.]]
+[[Category: Jackson DG]]
-[[Category: Jackson, D G.]]
+[[Category: Mahoney DJ]]
-[[Category: Mahoney, D J.]]
+[[Category: Noble MEM]]
-[[Category: Noble, M E.M.]]
+[[Category: Wright AJ]]
-[[Category: Wright, A J.]]
-[[Category: Alternative splicing]]
-[[Category: Antigen]]
-[[Category: Blood group antigen]]
-[[Category: C-type lectin]]
-[[Category: Cell adhesion]]
-[[Category: Extracellular matrix]]
-[[Category: Glycoprotein]]
-[[Category: Hyauronan]]
-[[Category: Lectin]]
-[[Category: Link-domain]]
-[[Category: Membrane]]
-[[Category: Phosphorylation]]
-[[Category: Polymorphism]]
-[[Category: Proteoglycan]]
-[[Category: Pyrrolidone carboxylic acid]]
-[[Category: Receptor]]
-[[Category: Sugar- binding]]
-[[Category: Sulfation]]
-[[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:42:25 2008''