Hyaluronan Recognition Mode of CD44 Revealed by Cross-saturation and Chemical Shift Perturbation Experiments

• Published in: The Journal of biological chemistry Vol. 278; no. 44; pp. 43550 - 43555
• Main Authors: Takeda, Mitsuhiro, Terasawa, Hiroaki, Sakakura, Masayoshi, Yamaguchi, Yoshiki, Kajiwara, Masahiro, Kawashima, Hiroto, Miyasaka, Masayuki, Shimada, Ichio
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 31.10.2003; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Binding Sites; Humans; Hyaluronan Receptors - chemistry; Hyaluronic Acid - chemistry; Hyaluronic Acid - metabolism; Ligands; Magnetic Resonance Spectroscopy; Models, Biological; Molecular Sequence Data; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid

CD44 is the main cell surface receptor for hyaluronic acid (HA) and contains a functional HA-binding domain (HABD) composed of a Link module with N- and C-terminal extensions. The contact residues of human CD44 HABD for HA have been determined by cross-saturation experiments and mapped on the topolo...