Ontology highlight
ABSTRACT:
SUBMITTER: Widmer C
PROVIDER: S-EPMC3421173 | biostudies-literature | 2012 Aug
REPOSITORIES: biostudies-literature
Widmer Christine C Gebauer Jan M JM Brunstein Elena E Rosenbaum Sabrina S Zaucke Frank F Drögemüller Cord C Leeb Tosso T Baumann Ulrich U
Proceedings of the National Academy of Sciences of the United States of America 20120730 33
Collagen is the most abundant protein in animals and is a major component of the extracellular matrix in tissues such as skin and bone. A distinctive structural feature of all collagen types is a unique triple-helical structure formed by tandem repeats of the consensus sequence Xaa-Yaa-Gly, in which Xaa and Yaa frequently are proline and hydroxyproline, respectively. Hsp47/SERPINH1 is a procollagen-specific molecular chaperone that, unlike other chaperones, specifically recognizes the folded con ...[more]