Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by FRANKEN, P.
Right arrow Articles by DUMAS, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by FRANKEN, P.
Right arrow Articles by DUMAS, C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 6, Issue 12 2681-2683, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

HIV-1 Nef protein: Purification, crystallizations, and preliminary X-ray diffraction studies

P. FRANKEN, S. AROLD, A. PADILLA, M. BODEUS, F. HOH, M. P. STRUB, M. BOYER, M. JULLIEN, R. BENAROUS and C. DUMAS
Centre de Biochimie Structurale, UMR C9955 CNRS, U414 INSERM, Universite Montpellier I, Faculte de Pharmacie, Avenue C. Flahault, 34060 Montpellier, France

Human immunodeficiency virus Nef protein accelerates virulent progression of AIDS by its interaction with specific cellular proteins involved in cellular activation and signal transduction. Here we report the purification and crystallization of the conserved core of HIV-1(LAI) Nef protein in the unliganded form and in complex with the wild-type SH3 domain of the p59(fyn) protein-tyrosine kinase. One-dimensional NMR experiments show that full-length protein and truncated fragment corresponding to the product of HIV-1 protease cleavage have a well-folded compact tertiary structure. The ligand-free HIV-1 Nef(core) protein forms cubic crystals belonging to space group P23 with unit cell dimensions of a = b = c = 86.4 A. The Nef-Fyn SH3 cocrystals belong to the space group P6(1)22 or its enantiomorph, P6(5)22, with unit cell dimensions of a = b = 108.2 A and c = 223.7 A. Both crystal forms diffract to a resolution limit of 3.0 A resolution using synchrotron radiation, and are thus suitable for X-ray structure determination.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Microbiol. Mol. Biol. Rev.Home page
J. F. Roeth and K. L. Collins
Human Immunodeficiency Virus Type 1 Nef: Adapting to Intracellular Trafficking Pathways
Microbiol. Mol. Biol. Rev., June 1, 2006; 70(2): 548 - 563.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
P. D'Aloja, A. C. Santarcangelo, S. Arold, A. Baur, and M. Federico
Genetic and functional analysis of the human immunodeficiency virus (HIV) type 1-inhibiting F12-HIVnef allele
J. Gen. Virol., November 1, 2001; 82(11): 2735 - 2745.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by The Protein Society.