1bde: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1bde.gif|left|200px]]
{{Seed}}
[[Image:1bde.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bde|  PDB=1bde  |  SCENE=  }}  
{{STRUCTURE_1bde|  PDB=1bde  |  SCENE=  }}  


'''HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES'''
===HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_9851370}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9851370 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9851370}}


==About this Structure==
==About this Structure==
1BDE is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDE OCA].  
1BDE is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDE OCA].  


==Reference==
==Reference==
Line 30: Line 34:
[[Category: Viral protein]]
[[Category: Viral protein]]
[[Category: Vpr fragment]]
[[Category: Vpr fragment]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:22:10 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:53:34 2008''

Revision as of 15:53, 30 June 2008

File:1bde.png

Template:STRUCTURE 1bde

HELICAL STRUCTURE OF POLYPEPTIDES FROM THE C-TERMINAL HALF OF HIV-1 VPR, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9851370

About this Structure

1BDE is a Single protein structure. Full experimental information is available from 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:9851370

Page seeded by OCA on Mon Jun 30 18:53:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1bde&oldid=577164"