1kzs
From Proteopedia
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| - | [[Image:1kzs.jpg|left|200px]] | + | [[Image:1kzs.jpg|left|200px]] |
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| - | '''Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE Solution''' | + | {{Structure |
| + | |PDB= 1kzs |SIZE=350|CAPTION= <scene name='initialview01'>1kzs</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE Solution''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KZS is a [ | + | 1KZS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZS OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution., Engler A, Stangler T, Willbold D, Eur J Biochem. 2002 Jul;269(13):3264-9. PMID:[http:// | + | Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution., Engler A, Stangler T, Willbold D, Eur J Biochem. 2002 Jul;269(13):3264-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12084067 12084067] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Engler, A.]] | [[Category: Engler, A.]] | ||
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[[Category: vpr]] | [[Category: vpr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:28 2008'' |
Revision as of 10:24, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE Solution
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.
About this Structure
1KZS is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution., Engler A, Stangler T, Willbold D, Eur J Biochem. 2002 Jul;269(13):3264-9. PMID:12084067
Page seeded by OCA on Thu Mar 20 12:24:28 2008
Categories: Single protein | Engler, A. | Stangler, T. | Willbold, D. | ACE | NH2 | Hiv-1 | Nmr | Peptide | Solution structure | Tfe | Vpr
