Amino acid requirement for the high affinity binding of a selected arginine-rich peptide with the HIV Rev-response element RNA

2008 ◽  
Vol 14 (8) ◽  
pp. 924-935 ◽  
Author(s):  
Maki Sugaya ◽  
Norikazu Nishino ◽  
Akira Katoh ◽  
Kazuo Harada
1998 ◽  
Vol 273 (26) ◽  
pp. 15927-15932 ◽  
Author(s):  
Eduardo Sainz ◽  
Mark Akeson ◽  
Samuel A. Mantey ◽  
Robert T. Jensen ◽  
James F. Battey

2010 ◽  
Vol 39 (7) ◽  
pp. 2931-2942 ◽  
Author(s):  
Maria A. Schumacher ◽  
Mareen Sprehe ◽  
Maike Bartholomae ◽  
Wolfgang Hillen ◽  
Richard G. Brennan

1990 ◽  
Vol 265 (3) ◽  
pp. 919-921 ◽  
Author(s):  
J B Clarke ◽  
E E Eliopoulos ◽  
J B C Findlay ◽  
P F Zagalsky

The apoproteins of the lobster carotenoprotein, crustacyanin, show single high-affinity binding sites for the hydrophobic fluorescence probes 8-anilo-1-naphthalenesulphonic acid and cis-parinaric acid, and exhibit fluorescence transfer from tryptophan to the ligands. These results, together with information from the amino acid sequences, infer that the native carotenoid, astaxanthin, is bound to each apoprotein within an internal hydrophobic pocket, or calyx.


Biochemistry ◽  
1998 ◽  
Vol 37 (49) ◽  
pp. 17287-17298 ◽  
Author(s):  
Iain Anderson ◽  
Christopher R. Bartley ◽  
Robert A. Lerch ◽  
Wesley G. N. Gray ◽  
Paul D. Friesen ◽  
...  

2002 ◽  
Vol 76 (10) ◽  
pp. 5140-5146 ◽  
Author(s):  
Christina F. Spiropoulou ◽  
Stefan Kunz ◽  
Pierre E. Rollin ◽  
Kevin P. Campbell ◽  
Michael B. A. Oldstone

ABSTRACT α-Dystroglycan (α-DG) has been identified as a major receptor for lymphocytic choriomeningitis virus (LCMV) and Lassa virus, two Old World arenaviruses. The situation with New World arenaviruses is less clear: previous studies demonstrated that Oliveros virus also exhibited high-affinity binding to α-DG but that Guanarito virus did not. To extend these initial studies, several additional Old and New World arenaviruses were screened for entry into mouse embryonic stem cells possessing or lacking α-DG. In addition, representative viruses were further analyzed for direct binding to α-DG by means of a virus overlay protein blot assay technique. These studies indicate that Old World arenaviruses use α-DG as a major receptor, whereas, of the New World arenaviruses, only clade C viruses (i.e., Oliveros and Latino viruses) use α-DG as a major receptor. New World clade A and B arenaviruses, which include the highly pathogenic Machupo, Guanarito, Junin, and Sabia viruses, appear to use a different receptor or coreceptor for binding. Previous studies with LCMV have suggested the need for a small aliphatic amino acid at LCMV GP1 glycoprotein amino acid position 260 to allow high-affinity binding to α-DG. As reported herein, this requirement appears to be broadly applicable to the arenaviruses as determined by more extensive analysis of α-DG receptor usage and GP1 sequences of Old and New World arenaviruses. In addition, GP1 amino acid position 259 also appears to be important, since all arenaviruses showing high-affinity α-DG binding possess a bulky aromatic amino acid (tyrosine or phenylalanine) at this position.


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