1bde: Difference between revisions
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[[Image:1bde.gif|left|200px]]< | [[Image:1bde.gif|left|200px]] | ||
'''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES''' | {{Structure | ||
|PDB= 1bde |SIZE=350|CAPTION= <scene name='initialview01'>1bde</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BDE is a [ | 1BDE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDE OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of peptides from HIV-1 Vpr protein that cause membrane permeabilization and growth arrest., Yao S, Torres AM, Azad AA, Macreadie IG, Norton RS, J Pept Sci. 1998 Nov;4(7):426-35. PMID:[http:// | Solution structure of peptides from HIV-1 Vpr protein that cause membrane permeabilization and growth arrest., Yao S, Torres AM, Azad AA, Macreadie IG, Norton RS, J Pept Sci. 1998 Nov;4(7):426-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9851370 9851370] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Azad, A A.]] | [[Category: Azad, A A.]] | ||
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[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: | [[Category: aid]] | ||
[[Category: helix]] | [[Category: helix]] | ||
[[Category: hiv]] | [[Category: hiv]] | ||
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[[Category: vpr fragment]] | [[Category: vpr fragment]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:30 2008'' | ||
Revision as of 11:09, 20 March 2008
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HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES
OverviewOverview
Vpr, one of the accessory gene products encoded by HIV-1, is a 96-residue protein with a number of functions, including targeting of the viral pre-integration complex to the nucleus and inducing growth arrest of dividing cells. We have characterized by 2D NMR the solution conformations of bioactive synthetic peptide fragments of Vpr encompassing a pair of H(F/S)RIG sequence motifs (residues 71-75 and 78-82 of HIV-1 Vpr) that cause cell membrane permeabilization and death in yeast and mammalian cells. Due to limited solubility of the peptides in water, their structures were studied in aqueous trifluoroethanol. Peptide Vpr59-86 (residues 59-86 of Vpr) formed an alpha-helix encompassing residues 60-77, with a kink in the vicinity of residue 62. The first of the repeated sequence motifs (HFRIG) participated in the well-defined alpha-helical domain whereas the second (HSRIG) lay outside the helical domain and formed a reverse turn followed by a less ordered region. On the other hand, peptides Vpr71-82 and Vpr71-96, in which the sequence motifs were located at the N-terminus, were largely unstructured under similar conditions, as judged by their C(alpha)H chemical shifts. Thus, the HFRIG and HSRIG motifs adopt alpha-helical and turn structures, respectively, when preceded by a helical structure, but are largely unstructured in isolation. The implications of these findings for interpretation of the structure-function relationships of synthetic peptides containing these motifs are discussed.
About this StructureAbout this Structure
1BDE is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of peptides from HIV-1 Vpr protein that cause membrane permeabilization and growth arrest., Yao S, Torres AM, Azad AA, Macreadie IG, Norton RS, J Pept Sci. 1998 Nov;4(7):426-35. PMID:9851370
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