1fi0
From Proteopedia
(New page: 200px<br /> <applet load="1fi0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fi0" /> '''SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEP...) |
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'''SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEPTIDE IN MICELLS'''<br /> | '''SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEPTIDE IN MICELLS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear | + | Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G2 cell cycle arrest and is involved in cellular differentiation and cell death. Also, 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 obviously is dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 13-33 of HIV-1 Vpr in micelles. Employing nuclear magnetic resonance and circular dichroism spectroscopy we found this part of Vpr, known to be essential for nuclear localization, to be almost completely alpha helical. Our results provide structural data suggesting residues 13-33 of Vpr to form an amphipathic, leucine-zipper-like alpha helix that serves as a basis for interactions with a variety of viral and cellular factors. |
==About this Structure== | ==About this Structure== | ||
| - | 1FI0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1FI0 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: helix]] | [[Category: helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:51 2008'' |
Revision as of 10:38, 21 February 2008
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SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEPTIDE IN MICELLS
Overview
Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G2 cell cycle arrest and is involved in cellular differentiation and cell death. Also, 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 obviously is dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 13-33 of HIV-1 Vpr in micelles. Employing nuclear magnetic resonance and circular dichroism spectroscopy we found this part of Vpr, known to be essential for nuclear localization, to be almost completely alpha helical. Our results provide structural data suggesting residues 13-33 of Vpr to form an amphipathic, leucine-zipper-like alpha helix that serves as a basis for interactions with a variety of viral and cellular factors.
About this Structure
1FI0 is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of human immunodeficiency virus type 1 Vpr(13-33) peptide in micelles., Engler A, Stangler T, Willbold D, Eur J Biochem. 2001 Jan;268(2):389-95. PMID:11168374
Page seeded by OCA on Thu Feb 21 12:38:51 2008
Categories: Single protein | Engler, A. | Stangler, T. | Willbold, D. | ACE | Helix
