Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.

ABSTRACT: The HIV gp41 protein catalyzes fusion between viral and host cell membranes, and its apolar N-terminal region or "fusion peptide" binds to the host cell membrane and plays a key role in fusion. "HFP" is a construct containing the fusion peptide sequence, induces membrane vesicle fusion, and is an important fusion model system. Earlier solid-state nuclear magnetic resonance (SSNMR) studies showed that when HFP is associated with membranes with ∼30 mol % cholesterol, the first 16 residues have predominant β strand secondary structure and a fraction of the strands form antiparallel β sheet structure with residue 16→1/1→16 or 17→1/1→17 registries for adjacent strands. In some contrast, other SSNMR and infrared studies have been interpreted to support a large fraction of an approximately in-reg

SUBMITTER: Schmick SD 

PROVIDER: S-EPMC3005821 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature