Structural and functional investigations of Matrilin-1 A-domains reveal insights into their role in cartilage ECM assembly.

ABSTRACT: Matrilin-1 is expressed predominantly in cartilage and co-localizes with matrilin-3 with which it can form hetero-oligomers. We recently described novel structural and functional features of the matrilin-3 A-domain (M3A) and demonstrated that it bound with high affinity to type II and IX collagens. Interactions preferentially occurred in the presence of Zn(2+) suggesting that matrilin-3 has acquired a requirement for specific metal ions for activation and/or molecular associations. To understand the interdependence of matrilin-1/-3 hetero-oligomers in extracellular matrix (ECM) interactions, we have extended these studies to include the two matrilin-1 A-domains (i.e. M1A1 and M1A2 respectively). In this study we have identified new characteristics of the matrilin-1 A-domains by describing

SUBMITTER: Fresquet M 

PROVIDER: S-EPMC2962504 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature