Investigation of pathways for the low-pH conformational transition in influenza hemagglutinin.

ABSTRACT: Targeted molecular dynamics simulations were used to study the conformational transition of influenza hemagglutinin (HA) from the native conformation to putative fusogenic or postfusion conformations populated at low pH. Three pathways for this conformational change were considered. Complete dissociation of the globular domains of HA was observed in one pathway, whereas smaller rearrangements were observed in the other two. The fusion peptides became exposed and moved toward the target membrane, although occasional movement toward the viral membrane was also observed. The effective energy profiles along the paths show multiple barriers. The final low-pH structures, which are consistent with available experimental data, are comparable in effective energy to native HA. As a control, the uncl

SUBMITTER: Madhusoodanan M 

PROVIDER: S-EPMC1302762 | biostudies-literature | 2003 Mar

REPOSITORIES: biostudies-literature