Distinguishing direct binding interactions from allosteric effects in the protease-HK97 prohead I δ domain complex by amide H/D exchange mass spectrometry.

ABSTRACT: A major question in mapping protein-ligand or protein-protein interactions in solution is to distinguish direct-binding interactions from long-range conformational changes at allosteric sites. We describe here the applicability of amide hydrogen deuterium exchange mass spectrometry (HDXMS) in addressing this important question using the bacteriophage HK97 capsid proteins' interactions with their processing protease. HK97 is a lambda-like dsDNA bacteriophage that is ideal for studies of particle assembly and maturation. Its capsid precursor protein is composed of two main regions, the scaffolding protein (δ-domain, residues 2-103), and the coat subunit (residues 104-385), which spontaneously forms a mixture of hexamers and pentamers upon association. Activation of the viral protease, which

SUBMITTER: Krishnamurthy S 

PROVIDER: S-EPMC4588519 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature