Ontology highlight
ABSTRACT:
SUBMITTER: Kaiserman D
PROVIDER: S-EPMC2666993 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Kaiserman Dion D Buckle Ashley M AM Van Damme Petra P Irving James A JA Law Ruby H P RH Matthews Antony Y AY Bashtannyk-Puhalovich Tanya T Langendorf Chris C Thompson Philip P Vandekerckhove Joël J Gevaert Kris K Whisstock James C JC Bird Phillip I PI
Proceedings of the National Academy of Sciences of the United States of America 20090319 14
Proteases act in important homeostatic pathways and are tightly regulated. Here, we report an unusual structural mechanism of regulation observed by the 2.5-A X-ray crystal structure of the serine protease, granzyme C. Although the active-site triad residues adopt canonical conformations, the oxyanion hole is improperly formed, and access to the primary specificity (S1) pocket is blocked through a reversible rearrangement involving Phe-191. Specifically, a register shift in the 190-strand preced ...[more]