Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding.

ABSTRACT: Decorin is the archetypal small leucine rich repeat proteoglycan of the vertebrate extracellular matrix (ECM). With its glycosaminoglycuronan chain, it is responsible for stabilizing inter-fibrillar organization. Type I collagen is the predominant member of the fibrillar collagen family, fulfilling both organizational and structural roles in animal ECMs. In this study, interactions between decoron (the decorin core protein) and binding sites in the d and e(1) bands of the type I collagen fibril were investigated through molecular modeling of their respective X-ray diffraction structures. Previously, it was proposed that a model-based, highly curved concave decoron interacts with a single collagen molecule, which would form extensive van der Waals contacts and give rise to strong non-specif

SUBMITTER: Orgel JP 

PROVIDER: S-EPMC2737631 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature