2JCP
The hyaluronan binding domain of murine CD44
Summary for 2JCP
Entry DOI | 10.2210/pdb2jcp/pdb |
Related | 2JCQ 2JCR |
Descriptor | CD44 ANTIGEN (2 entities in total) |
Functional Keywords | sugar-binding protein, hyauronan, link-domain, proteoglycan, polymorphism, blood group antigen, alternative splicing, lectin, antigen, membrane, receptor, sulfation, glycoprotein, c-type lectin, cell adhesion, extracellular matrix, pyrrolidone carboxylic acid, transmembrane, phosphorylation, sugar binding protein |
Biological source | MUS MUSCULUS (MOUSE) |
Total number of polymer chains | 1 |
Total formula weight | 17143.07 |
Authors | Banerji, S.,Wright, A.J.,Noble, M.E.M.,Mahoney, D.J.,Campbell, I.D.,Day, A.J.,Jackson, D.G. (deposition date: 2007-01-03, release date: 2007-01-30, Last modification date: 2024-02-07) |
Primary citation | Banerji, S.,Wright, A.J.,Noble, M.E.M.,Mahoney, D.J.,Campbell, I.D.,Day, A.J.,Jackson, D.G. Structures of the Cd44-Hyaluronan Complex Provide Insight Into a Fundamental Carbohydrate-Protein Interaction. Nat.Struct.Mol.Biol., 14:234-, 2008 Cited by PubMed Abstract: 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. PubMed: 17293874DOI: 10.1038/NSMB1201 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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