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| - | [[Image:1bm4.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1bm4| PDB=1bm4 | SCENE= }} | | {{STRUCTURE_1bm4| PDB=1bm4 | SCENE= }} |
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| - | '''MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG'''
| + | ===MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9799104}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9799104 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9799104}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1BM4 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM4 OCA]. | + | 1BM4 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM4 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Momlv]] | | [[Category: Momlv]] |
| | [[Category: Mu-mlv]] | | [[Category: Mu-mlv]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:41:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:22:21 2008'' |
Revision as of 16:22, 30 June 2008
Template:STRUCTURE 1bm4
MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG
Template:ABSTRACT PUBMED 9799104
About this Structure
1BM4 is a Single protein structure. Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Mon Jun 30 19:22:21 2008
