Structural characterization of mumps virus fusion protein core. Biochem Biophys Res Commun 2006 Sep 29;348(3):916-22
Date
08/15/2006Pubmed ID
16904649Pubmed Central ID
PMC7092830DOI
10.1016/j.bbrc.2006.07.168Scopus ID
2-s2.0-33747191789 (requires institutional sign-in at Scopus site) 11 CitationsAbstract
The fusion proteins of enveloped viruses mediating the fusion between the viral and cellular membranes comprise two discontinuous heptad repeat (HR) domains located at the ectodomain of the enveloped glycoproteins. The crystal structure of the fusion protein core of Mumps virus (MuV) was determined at 2.2 A resolution. The complex is a six-helix bundle in which three HR1 peptides form a central highly hydrophobic coiled-coil and three HR2 peptides pack against the hydrophobic grooves on the surface of central coiled-coil in an oblique antiparallel manner. Fusion core of MuV, like those of simian virus 5 and human respiratory syncytium virus, forms typical 3-4-4-4-3 spacing. The similar characterization in HR1 regions, as well as the existence of O-X-O motif in extended regions of HR2 helix, suggests a basic rule for the formation of the fusion core of viral fusion proteins.
Author List
Liu Y, Xu Y, Lou Z, Zhu J, Hu X, Gao GF, Qiu B, Rao Z, Tien PAuthor
Jieqing Zhu PhD Assistant Professor, Associate Investigator in the Biochemistry department at BloodCenter of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceConserved Sequence
Crystallography, X-Ray
Membrane Fusion
Molecular Sequence Data
Mumps virus
Parainfluenza Virus 5
Peptide Fragments
Protein Conformation
Protein Structure, Secondary
Repetitive Sequences, Amino Acid
Viral Fusion Proteins
