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'''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES''' | '''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES''' | ||
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==About this Structure== | ==About this Structure== | ||
1BDE is a [[Single protein]] structure | 1BDE is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Norton, R S.]] | [[Category: Norton, R S.]] | ||
[[Category: Yao, S.]] | [[Category: Yao, S.]] | ||
[[Category: | [[Category: Aid]] | ||
[[Category: | [[Category: Helix]] | ||
[[Category: | [[Category: Hiv]] | ||
[[Category: | [[Category: Viral protein]] | ||
[[Category: | [[Category: Vpr fragment]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:22:10 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 11:22, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 11:22:10 2008