1kzt: Difference between revisions

Line 4:

==Overview==

Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear, entry of viral nucleic acids in nondividing cells, causes G(2) cell cycle, arrest and is involved in cellular differentiation and cell death. Vpr, subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the, nuclear envelope of human cells. Further, a reported ion channel activity, of Vpr is clearly dependent on its localization in or at membranes. We, focused our structural studies on the secondary structure of a peptide, consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an, important role in Vpr oligomerization, contributes to cell cycle arrest, activity, and is essential for virion incorporation and binding to HHR23A, a protein involved in DNA repair. Employing NMR spectroscopy we found this, part of Vpr to be almost completely alpha helical in the presence of, micelles, as well as in trifluoroethanol containing and, methanol/chloroform solvent. Our results provide structural data, suggesting residues 34-51 of Vpr to contain an amphipathic, leucine-zipper-like alpha helix, which serves as a basis for, oligomerization of Vpr and its interactions with cellular and viral, factors involved in subcellular localization and virion incorporation of, Vpr.

Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G(2) cell cycle arrest and is involved in cellular differentiation and cell death. Vpr subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the nuclear envelope of human cells. Further, a reported ion channel activity of Vpr is clearly dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an important role in Vpr oligomerization, contributes to cell cycle arrest activity, and is essential for virion incorporation and binding to HHR23A, a protein involved in DNA repair. Employing NMR spectroscopy we found this part of Vpr to be almost completely alpha helical in the presence of micelles, as well as in trifluoroethanol containing and methanol/chloroform solvent. Our results provide structural data suggesting residues 34-51 of Vpr to contain an amphipathic, leucine-zipper-like alpha helix, which serves as a basis for oligomerization of Vpr and its interactions with cellular and viral factors involved in subcellular localization and virion incorporation of Vpr.

==About this Structure==

Line 25:

[[Category: vpr]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:15:56 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:43 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear, entry of viral nucleic acids in nondividing cells, causes G(2) cell cycle, arrest and is involved in cellular differentiation and cell death. Vpr, subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the, nuclear envelope of human cells. Further, a reported ion channel activity, of Vpr is clearly dependent on its localization in or at membranes. We, focused our structural studies on the secondary structure of a peptide, consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an, important role in Vpr oligomerization, contributes to cell cycle arrest, activity, and is essential for virion incorporation and binding to HHR23A, a protein involved in DNA repair. Employing NMR spectroscopy we found this, part of Vpr to be almost completely alpha helical in the presence of, micelles, as well as in trifluoroethanol containing and, methanol/chloroform solvent. Our results provide structural data, suggesting residues 34-51 of Vpr to contain an amphipathic, leucine-zipper-like alpha helix, which serves as a basis for, oligomerization of Vpr and its interactions with cellular and viral, factors involved in subcellular localization and virion incorporation of, Vpr.
+Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G(2) cell cycle arrest and is involved in cellular differentiation and cell death. Vpr subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the nuclear envelope of human cells. Further, a reported ion channel activity of Vpr is clearly dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an important role in Vpr oligomerization, contributes to cell cycle arrest activity, and is essential for virion incorporation and binding to HHR23A, a protein involved in DNA repair. Employing NMR spectroscopy we found this part of Vpr to be almost completely alpha helical in the presence of micelles, as well as in trifluoroethanol containing and methanol/chloroform solvent. Our results provide structural data suggesting residues 34-51 of Vpr to contain an amphipathic, leucine-zipper-like alpha helix, which serves as a basis for oligomerization of Vpr and its interactions with cellular and viral factors involved in subcellular localization and virion incorporation of Vpr.
 ==About this Structure==
@@ Line 25: / Line 25: @@
 [[Category: vpr]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:15:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:43 2008''