Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex.

ABSTRACT:

Background

To study the organization and interaction with the fusion domain (or fusion peptide, FP) of the transmembrane domain (TMD) of influenza virus envelope glycoprotein for its role in membrane fusion which is also essential in the cellular trafficking of biomolecules and sperm-egg fusion.

Results

The fluorescence and gel electrophoresis experiments revealed a tight self-assembly of TMD in the model membrane. A weak but non-random interaction between TMD and FP in the membrane was found. In the complex, the central TMD oligomer was packed by FP in an antiparallel fashion. FP insertion into the membrane was altered by binding to TMD. An infrared study exhibited an enhanced membrane perturbation by the complex formation. A model was built to illustrate the role of TMD in

SUBMITTER: Chang DK 

PROVIDER: S-EPMC2267159 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature