1bde: Difference between revisions

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<applet load="1bde" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1bde" />

'''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1BDE OCA].

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==

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: Azad, A.A.]]

[[Category: Azad, A A.]]

[[Category: Macreadie, I.G.]]

[[Category: Macreadie, I G.]]

[[Category: Norton, R.S.]]

[[Category: Norton, R S.]]

[[Category: Yao, S.]]

[[Category: ACE]]

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[[Category: vpr fragment]]

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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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1bde" />
 '''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES'''<br />
 ==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.
+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==
-BDE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BDE OCA].
+BDE 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==
 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: Azad, A.A.]]
+[[Category: Azad, A A.]]
-[[Category: Macreadie, I.G.]]
+[[Category: Macreadie, I G.]]
-[[Category: Norton, R.S.]]
+[[Category: Norton, R S.]]
 [[Category: Yao, S.]]
 [[Category: ACE]]
@@ Line 25: / Line 24: @@
 [[Category: vpr fragment]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 13:53:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:04 2008''