2fyz: Difference between revisions

Revision as of 18:26, 21 February 2008

Structural of Mumps virus fusion protein core

OverviewOverview

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.

About this StructureAbout this Structure

2FYZ is a Protein complex structure of sequences from Mumps virus. Full crystallographic information is available from OCA.

ReferenceReference

Structural characterization of mumps virus fusion protein core., Liu Y, Xu Y, Lou Z, Zhu J, Hu X, Gao GF, Qiu B, Rao Z, Tien P, Biochem Biophys Res Commun. 2006 Sep 29;348(3):916-22. Epub 2006 Aug 4. PMID:16904649

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: mumps virus fusion protein core]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:33 2008''