Ontology highlight
ABSTRACT:
SUBMITTER: Kumar L
PROVIDER: S-EPMC7692495 | biostudies-literature | 2020 Nov
REPOSITORIES: biostudies-literature
Kumar Lokender L Planas-Iglesias Joan J Harms Chase C Kamboj Sumaer S Wright Derek D Klein-Seetharaman Judith J Sarkar Susanta K SK
Scientific reports 20201126 1
The roles of protein conformational dynamics and allostery in function are well-known. However, the roles that interdomain dynamics have in function are not entirely understood. We used matrix metalloprotease-1 (MMP1) as a model system to study the relationship between interdomain dynamics and activity because MMP1 has diverse substrates. Here we focus on fibrin, the primary component of a blood clot. Water-soluble fibrinogen, following cleavage by thrombin, self-polymerize to form water-insolub ...[more]