Integrin Activation State Determines Selectivity for Novel Recognition Sites in Fibrillar Collagens

• Published in: The Journal of biological chemistry Vol. 279; no. 46; pp. 47763 - 47772
• Main Authors: Siljander, Pia R-M, Hamaia, Samir, Peachey, Anthony R, Slatter, David A, Smethurst, Peter A, Ouwehand, Willem H, Knight, C Graham, Farndale, Richard W
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 12.11.2004
• Subjects: Amino Acid Motifs; Animals; Blood Platelets - metabolism; Cell Line; Collagen Type I - chemistry; Collagen Type I - genetics; Collagen Type I - metabolism; Humans; Integrin alpha Chains - genetics; Integrin alpha Chains - metabolism; Integrin alpha2beta1 - genetics; Integrin alpha2beta1 - metabolism; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; Platelet Adhesiveness - physiology; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Sequence Alignment

Only three recognition motifs, GFOGER, GLOGER, and GASGER, all present in type I collagen, have been identified to date for collagen-binding integrins, such as α 2 β 1 . Sequence alignment was used to investigate the occurrence of related motifs in other human fibrillar collagens, and located a co...