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1mof

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Revision as of 10:22, 25 October 2017

COAT PROTEIN

Structural highlights

1mof is a 1 chain structure with sequence from Mlvmo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ENV_MLVMS] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. Interaction with HECT ubiquitin ligases activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane.^[1] The transmembrane protein (TM) acts as a 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 target cell membrane fusion, the coiled coil regions (heptad repeats) 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 target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (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

We report the crystal structure of an extraviral segment of a retrovirus envelope protein, the Moloney murine leukemia virus (MoMuLV) transmembrane (TM) subunit. This segment, which comprises a region of the MoMuLV TM protein analogous to that contained within the X-ray crystal structure of low-pH converted influenza hemagglutinin, contains a trimeric coiled coil, with a hydrophobic cluster at its base and a strand that packs in an antiparallel orientation against the coiled coil. This structure gives the first high-resolution insight into the retrovirus surface and serves as a model for a wide range of viral fusion proteins; key residues in this structure are conserved among C- and D-type retroviruses and the filovirus ebola.

Retrovirus envelope domain at 1.7 angstrom resolution.,Fass D, Harrison SC, Kim PS Nat Struct Biol. 1996 May;3(5):465-9. PMID:8612078^[2]

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

References

↑ Wu SR, Sjoberg M, Wallin M, Lindqvist B, Ekstrom M, Hebert H, Koeck PJ, Garoff H. Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion. EMBO J. 2008 Oct 22;27(20):2799-808. doi: 10.1038/emboj.2008.187. Epub 2008 Sep, 18. PMID:18800055 doi:http://dx.doi.org/10.1038/emboj.2008.187
↑ Fass D, Harrison SC, Kim PS. Retrovirus envelope domain at 1.7 angstrom resolution. Nat Struct Biol. 1996 May;3(5):465-9. PMID:8612078

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/1mof"

@@ Line 1: / Line 1: @@
 ==COAT PROTEIN==
 <StructureSection load='1mof' size='340' side='right' caption='[[1mof]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1mof]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mlvmo Mlvmo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MOF FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=1mof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mof OCA], [http://pdbe.org/1mof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mof RCSB], [http://www.ebi.ac.uk/pdbsum/1mof 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=1mof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mof OCA], [http://pdbe.org/1mof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mof RCSB], [http://www.ebi.ac.uk/pdbsum/1mof PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mof ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mof ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1mof

From Proteopedia

Revision as of 10:22, 25 October 2017

COAT PROTEIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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