COMP and TSP-4 interact specifically with the novel GXKGHR motif only found in fibrillar collagens.

ABSTRACT: COMP (cartilage oligomeric matrix protein) is a member of the thrombospondin family and forms homopentamers as well as mixed heterooligomers with its closely related family member TSP-4. COMP is long known to bind to collagens and to influence collagen fibril formation. Recent work indicates that already intracellular interaction with collagen is important for collagen secretion. However, the exact binding site of COMP on the collagen triple helix has not been described up to now. In this study we have identified a GXKGHR motif on the collagen II helix to bind to COMP, using a recombinantly expressed collagen II peptide library. This binding sequence is conserved throughout evolution and we demonstrate that TSP-4 binds to the same sequence. The identified binding motif overlaps with the re

SUBMITTER: Gebauer JM 

PROVIDER: S-EPMC6249252 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature