Ontology highlight
ABSTRACT:
SUBMITTER: Wirz JA
PROVIDER: S-EPMC3048825 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Wirz Jacqueline A JA Boudko Sergei P SP Lerch Thomas F TF Chapman Michael S MS Bächinger Hans Peter HP
Matrix biology : journal of the International Society for Matrix Biology 20101013 1
Correct folding of the collagen triple helix requires a self-association step which selects and binds α-chains into trimers. Here we report the crystal structure of the trimerization domain of human type XV collagen. The trimerization domain of type XV collagen contains three monomers each composed of four β-sheets and an α-helix. The hydrophobic core of the trimer is devoid of solvent molecules and is shaped by β-sheet planes from each monomer. The trimerization domain is extremely stable and f ...[more]