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1bde
From Proteopedia
(New page: 200px<br /> <applet load="1bde" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bde" /> '''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE ...) |
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| - | [[Image:1bde.gif|left|200px]]<br /> | + | [[Image:1bde.gif|left|200px]]<br /><applet load="1bde" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bde" size=" | + | |
caption="1bde" /> | caption="1bde" /> | ||
'''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES'''<br /> | '''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Vpr, one of the accessory gene products encoded by HIV-1, is a 96-residue | + | 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 Structure== | ==About this Structure== | ||
| - | 1BDE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1BDE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9851370 9851370] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9851370 9851370] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Azad, A | + | [[Category: Azad, A A.]] |
| - | [[Category: Macreadie, I | + | [[Category: Macreadie, I G.]] |
| - | [[Category: Norton, R | + | [[Category: Norton, R S.]] |
[[Category: Yao, S.]] | [[Category: Yao, S.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
| Line 25: | Line 24: | ||
[[Category: vpr fragment]] | [[Category: vpr fragment]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:04 2008'' |
Revision as of 09:54, 21 February 2008
|
HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES
Overview
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 Structure
1BDE is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.
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:9851370
Page seeded by OCA on Thu Feb 21 11:54:04 2008
Categories: Single protein | Azad, A A. | Macreadie, I G. | Norton, R S. | Yao, S. | ACE | NH2 | Aids | Helix | Hiv | Viral protein | Vpr fragment
