2pjv: Difference between revisions
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==solution structure of hiv-1 gp41 fusion domain bound to DPC micelle== | |||
<StructureSection load='2pjv' size='340' side='right'caption='[[2pjv]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2pjv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PJV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pjv OCA], [https://pdbe.org/2pjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pjv RCSB], [https://www.ebi.ac.uk/pdbsum/2pjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pjv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A1YNH3_9HIV1 A1YNH3_9HIV1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A thorough understanding of the structure of fusion domains of enveloped viruses in changing lipid environments helps us to formulate mechanistic models on how they might function in mediating viral entry by membrane fusion. We have expressed the N-terminal fusion domain of HIV-1 gp41 as a construct that is water-soluble in the absence of membranes, but that also binds with high affinity to lipid micelles and bilayers in their presence. We have solved the structure and studied the dynamics of this domain bound to dodecylphosphocholine micelles by homo- and heteronuclear NMR spectroscopy. The fusion peptide forms a stable hydrophobic helix from Ile(4) to Ala(14), but is increasingly more disordered and dynamic in a segment of intermediate polarity that stretches from Ala(15) to Ser(23). When bound to lipid bilayers at low concentration, the HIV fusion domain is also largely alpha-helical, as determined by CD and FTIR spectroscopy. However, at higher protein/lipid ratios, the domain is partially converted to form beta-structures in lipid bilayers. Controlled lipid mixing occurs at concentrations that support the alpha-helical, but not the beta-strand conformation. | |||
Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers.,Li Y, Tamm LK Biophys J. 2007 Aug 1;93(3):876-85. Epub 2007 May 18. PMID:17513369<ref>PMID:17513369</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2pjv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Li Y]] | ||
[[Category: | [[Category: Tamm LK]] | ||
Latest revision as of 16:10, 26 July 2023
solution structure of hiv-1 gp41 fusion domain bound to DPC micellesolution structure of hiv-1 gp41 fusion domain bound to DPC micelle
Structural highlights
FunctionPublication Abstract from PubMedA thorough understanding of the structure of fusion domains of enveloped viruses in changing lipid environments helps us to formulate mechanistic models on how they might function in mediating viral entry by membrane fusion. We have expressed the N-terminal fusion domain of HIV-1 gp41 as a construct that is water-soluble in the absence of membranes, but that also binds with high affinity to lipid micelles and bilayers in their presence. We have solved the structure and studied the dynamics of this domain bound to dodecylphosphocholine micelles by homo- and heteronuclear NMR spectroscopy. The fusion peptide forms a stable hydrophobic helix from Ile(4) to Ala(14), but is increasingly more disordered and dynamic in a segment of intermediate polarity that stretches from Ala(15) to Ser(23). When bound to lipid bilayers at low concentration, the HIV fusion domain is also largely alpha-helical, as determined by CD and FTIR spectroscopy. However, at higher protein/lipid ratios, the domain is partially converted to form beta-structures in lipid bilayers. Controlled lipid mixing occurs at concentrations that support the alpha-helical, but not the beta-strand conformation. Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers.,Li Y, Tamm LK Biophys J. 2007 Aug 1;93(3):876-85. Epub 2007 May 18. PMID:17513369[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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