1kzs
From Proteopedia
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|PDB= 1kzs |SIZE=350|CAPTION= <scene name='initialview01'>1kzs</scene> | |PDB= 1kzs |SIZE=350|CAPTION= <scene name='initialview01'>1kzs</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kzt|1KZT]], [[1kzv|1KZV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzs OCA], [http://www.ebi.ac.uk/pdbsum/1kzs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kzs RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Stangler, T.]] | [[Category: Stangler, T.]] | ||
[[Category: Willbold, D.]] | [[Category: Willbold, D.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NH2]] | ||
[[Category: hiv-1]] | [[Category: hiv-1]] | ||
[[Category: nmr]] | [[Category: nmr]] | ||
| Line 33: | Line 34: | ||
[[Category: vpr]] | [[Category: vpr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:55:55 2008'' |
Revision as of 18:55, 30 March 2008
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| Ligands: | , | ||||||
| Related: | 1KZT, 1KZV
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 21:55:55 2008
Categories: Single protein | Engler, A. | Stangler, T. | Willbold, D. | Hiv-1 | Nmr | Peptide | Solution structure | Tfe | Vpr
