View source for 1bmx


==HIV-1 CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG, NMR, 8 STRUCTURES==
<StructureSection load='1bmx' size='340' side='right'caption='[[1bmx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bmx]] 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=1BMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMX 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=1bmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmx OCA], [https://pdbe.org/1bmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bmx RCSB], [https://www.ebi.ac.uk/pdbsum/1bmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bmx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q76258_9HIV1 Q76258_9HIV1] 
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== Publication Abstract from PubMed ==
The capsid domain of retroviral Gag proteins possesses a single highly conserved subdomain termed the major homology region (MHR). While the mutagenesis of residues in the MHR will impair virus infectivity, the precise solution structure and function of the MHR is not known. To aid the structure/function characterization of the MHR, the structures of synthetic peptides encompassing the MHR of the human immunodeficiency virus type I (HIV-1) and Moloney murine leukemia virus (MoMLV) capsid proteins were investigated by several techniques. Homology-based secondary-structure prediction suggested that the HIV-1 and MoMLV peptides could form 50% and 38% alpha-helix, respectively. CD studies indicated that, in the presence of 50% trifluoroethanol, the HIV-1 peptide adopts an alpha-helical structure over half of its length, while the MoMLV peptide is over one third alpha-helix. Further analysis by 1H-NMR suggested that the C-terminal portion of the MHR of each virus forms a helix in aqueous solution. Distance-geometry structures of each peptide were calculated from NOE distance restraints and were refined by restrained molecular dynamics. The C-terminal halves of both peptides were observed to be in an alpha-helical conformation, while the N-terminal halves were disordered. Furthermore, both helices were amphipathic with high conservation of amino acid side-chain character, suggesting that a conserved helical MHR C-terminus is essential to retroviral capsid protein function.

Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy.,Clish CB, Peyton DH, Barklis E Eur J Biochem. 1998 Oct 1;257(1):69-77. PMID:9799104<ref>PMID:9799104</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Barklis E]]
[[Category: Clish CB]]
[[Category: Peyton DH]]