The structural basis of mode of activation and functional diversity: a case study with HtrA family of serine proteases.

Nitu Singh, Raja R Kuppili, Kakoli Bose

Journal: Archives of biochemistry and biophysics 2012;516(2):85-96

PMID: 22027029

Full Text on Elsevier Science View on PubMed

Abstract

HtrA (High temperature requirement protease A) proteins that are primarily involved in protein quality control belong to a family of serine proteases conserved from bacteria to humans. HtrAs are oligomeric proteins that share a common trimeric pyramidal architecture where each monomer comprises a serine protease domain and one or two PDZ domains. Although the overall structural integrity is well maintained and they exhibit similar mechanism of activation, subtle conformational changes and structural plasticity especially in the flexible loop regions and domain interfaces lead to differences in their active site conformation and hence in their specificity and functions.

Address: Advanced Centre for Treatment, Research and Education in Cancer (ACTREC), Tata Memorial Centre, Kharghar, Navi Mumbai, India.

DOI: 10.1016/j.abb.2011.10.007