Strand 6B deformation and residues exposure towards N-terminal end of helix B during proteinase inhibition by Serpins.

ABSTRACT:

Unlabelled

Serine Protease inhibitors (Serpins) like antithrombin, antitrypsin, neuroserpin, antichymotrypsin, protein C-inhibitor and plasminogen activator inhibitor is involved in important biological functions like blood coagulation, fibrinolysis, inflammation, cell migration and complement activation. Serpins native state is metastable, which undergoes transformation to a more stable state during the process of protease inhibition. Serpins are prone to conformation defects, however little is known about the factors and mechanisms which promote its conformational change and misfolding. Helix B region in serpins is with several point mutations which result in pathological conditions due to polymerization. Helix B analysis for residue burial and cavity was undertaken to understand

SUBMITTER: Singh P 

PROVIDER: S-EPMC3046034 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature