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1g2c

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Revision as of 17:05, 10 September 2015

HUMAN RESPIRATORY SYNCYTIAL VIRUS FUSION PROTEIN CORE

Structural highlights

1g2c is a 24 chain structure with sequence from Hrsvr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	HRSV F (HRSVR)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[FUS_HRSVR] Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human respiratory syncytial virus (HRSV) is a major cause of a number of severe respiratory diseases, including bronchiolitis and pneumonia, in infants and young children. The HRSV F protein, a glycoprotein essential for viral entry, is a primary target for vaccine and drug development. Two heptad-repeat regions within the HRSV F sequence were predicted by the computer program learncoil-vmf. These regions are thought to form trimer-of-hairpins-like structures, similar to those found in the fusion proteins of several enveloped viruses. The hairpin structure likely brings the viral and cellular membranes into close apposition, thereby facilitating membrane fusion and subsequent viral entry. Here, we show that peptides, denoted HR-N and HR-C, corresponding to the heptad-repeat regions from the N-terminal and C-terminal segments of the HRSV F protein, respectively, form a stable alpha-helical trimer of heterodimers. The HRSV N/C complex was crystallized and its x-ray structure was determined at 2.3-A resolution. As anticipated, the complex is a six-helix bundle in which the HR-N peptides form a three-stranded, central coiled coil, and the HR-C peptides pack in an antiparallel manner into hydrophobic grooves on the coiled-coil surface. There is remarkable structural similarity between the HRSV N/C complex and the fusion protein core of other viruses, including HIV-1 gp41. In addition, earlier work has shown that HRSV HR-C peptides, like the HIV-1 gp41 C peptides, inhibit viral infection. Thus, drug discovery and vaccine development strategies aimed at inhibiting viral entry by blocking hairpin formation may be applied to the inhibition of HRSV.

Structural characterization of the human respiratory syncytial virus fusion protein core.,Zhao X, Singh M, Malashkevich VN, Kim PS Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14172-7. PMID:11106388^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhao X, Singh M, Malashkevich VN, Kim PS. Structural characterization of the human respiratory syncytial virus fusion protein core. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14172-7. PMID:11106388 doi:10.1073/pnas.260499197

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g2c"

@@ Line 2: / Line 2: @@
 <StructureSection load='1g2c' size='340' side='right' caption='[[1g2c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1g2c]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_respiratory_syncytial_virus_strain_rss-2 Human respiratory syncytial virus strain rss-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G2C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1g2c]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrsvr Hrsvr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G2C FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HRSV F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11261 Human respiratory syncytial virus strain RSS-2])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HRSV F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11261 HRSVR])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g2c RCSB], [http://www.ebi.ac.uk/pdbsum/1g2c PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2c OCA], [http://pdbe.org/1g2c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g2c RCSB], [http://www.ebi.ac.uk/pdbsum/1g2c PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1g2c" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human respiratory syncytial virus strain rss-2]]
+[[Category: Hrsvr]]
 [[Category: Kim, P S]]
 [[Category: Malashkevich, V N]]

1g2c

From Proteopedia

Revision as of 17:05, 10 September 2015

HUMAN RESPIRATORY SYNCYTIAL VIRUS FUSION PROTEIN CORE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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