2jcr: Difference between revisions

Revision as of 08:44, 7 May 2008

THE HYALURONAN BINDING DOMAIN OF MURINE CD44 IN A TYPE B COMPLEX WITH AN HA 8-MER

OverviewOverview

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.

About this StructureAbout this Structure

2JCR is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Wed May 7 08:44:40 2008

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OCA

@@ Line 11: / Line 11: @@
 '''THE HYALURONAN BINDING DOMAIN OF MURINE CD44 IN A TYPE B COMPLEX WITH AN HA 8-MER'''
+==Overview==
+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.
 ==About this Structure==
 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].
+==Reference==
+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:[http://www.ncbi.nlm.nih.gov/pubmed/17293874 17293874]
 [[Category: Mus musculus]]
 [[Category: Single protein]]
@@ Line 39: / Line 45: @@
 [[Category: Pyrrolidone carboxylic acid]]
 [[Category: Receptor]]
-[[Category: Sugar- binding]]
+[[Category: Sugar-binding]]
+[[Category: Sugar-binding protein]]
 [[Category: Sulfation]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:42:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  7 08:44:40 2008''