Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 417, Issue 1, Pages 268-273Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.11.098
Keywords
Mtb; Acr; sHSP; alpha-Crystallin; Molecular dynamics; Dehydron
Categories
Funding
- Welch Foundation [BH-0018]
Ask authors/readers for more resources
Molecular dynamics simulations of a fitted multimeric structure of Mycobacterium tuberculosis alpha-crystallin (Mtb Acr) identify solvent exclusion from the beta(4)-beta(8) hydrophobic groove as a critical factor driving subunit assembly. Dehydration is also implicated as a determinant factor governing the chaperone activity of the dimer upon its dissociation from the oligomer. Two exposed hydrogen bonds, responsible for stabilizing the beta(8)-beta(9) fold are identified as key mechanistic elements in this process. Based on the overproduction of the chemokine CXCL16, observed after macrophage exposure to Mtb Acr, the proteases ADAM10 and ADAM17 are mooted as possible targets of this chaperone activity. (C) 2011 Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available