scholarly journals An Extended LXXLL Motif Sequence Determines the Nuclear Receptor Binding Specificity of TRAP220

2003 ◽  
Vol 278 (13) ◽  
pp. 10942-10951 ◽  
Author(s):  
Victoria H. Coulthard ◽  
Sachiko Matsuda ◽  
David M. Heery
Keyword(s):  
Nuclear Receptor ◽  
Receptor Binding ◽  
Binding Specificity ◽  
Lxxll Motif ◽  
Receptor Binding Specificity

High-Resolution Structure of Murine Interleukin 1 Homologue IL-1F5 Reveals Unique Loop Conformations for Receptor Binding Specificity†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (37) ◽  
pp. 10938-10944 ◽  
Author(s):  
Eleanor F. Dunn ◽  
Nicholas J. Gay ◽  
Adrian F. Bristow ◽  
David P. Gearing ◽  
Luke A. J. O'Neill ◽  
...  
Keyword(s):  
High Resolution ◽  
Receptor Binding ◽  
Interleukin 1 ◽  
Binding Specificity ◽  
Loop Conformations ◽  
High Resolution Structure ◽  
Receptor Binding Specificity ◽  
Resolution Structure

scholarly journals Highly Pathogenic Influenza A(H5Nx) Viruses with Altered H5 Receptor-Binding Specificity

2017 ◽  
Vol 23 (2) ◽  
pp. 220-231 ◽  
Author(s):  
Hongbo Guo ◽  
Erik de Vries ◽  
Ryan McBride ◽  
Jojanneke Dekkers ◽  
Wenjie Peng ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Influenza A ◽  
Binding Specificity ◽  
Highly Pathogenic ◽  
Receptor Binding Specificity

scholarly journals Receptor-Binding Specificity Depending on N-terminal Structure of VIP/PACAP

1999 ◽  
Vol 20 (4) ◽  
pp. 219-231 ◽  
Author(s):  
SATOMI ONOUE ◽  
YUMIKO NAGANO ◽  
ICHIRO TATSUNO ◽  
DAIGAKU UCHIDA ◽  
KAZUHISA KASHIMOTO
Keyword(s):  
Receptor Binding ◽  
Binding Specificity ◽  
Terminal Structure ◽  
Receptor Binding Specificity

scholarly journals Neuraminidase Inhibitor Sensitivity and Receptor-Binding Specificity of Cambodian Clade 1 Highly Pathogenic H5N1 Influenza Virus

2011 ◽  
Vol 55 (5) ◽  
pp. 2004-2010 ◽  
Author(s):  
M. Naughtin ◽  
J. C. Dyason ◽  
S. Mardy ◽  
S. Sorn ◽  
M. von Itzstein ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Receptor Binding ◽  
Reverse Genetics ◽  
Binding Specificity ◽  
Neuraminidase Inhibitor ◽  
H5n1 Influenza Virus ◽  
Highly Pathogenic ◽  
H5n1 Influenza ◽  
Receptor Binding Specificity ◽  
Pathogenic H5n1

ABSTRACTThe evolution of the highly pathogenic H5N1 influenza virus produces genetic variations that can lead to changes in antiviral susceptibility and in receptor-binding specificity. In countries where the highly pathogenic H5N1 virus is endemic or causes regular epidemics, the surveillance of these changes is important for assessing the pandemic risk. In Cambodia between 2004 and 2010, there have been 26 outbreaks of highly pathogenic H5N1 influenza virus in poultry and 10 reported human cases, 8 of which were fatal. We have observed naturally occurring mutations in hemagglutinin (HA) and neuraminidase (NA) of Cambodian H5N1 viruses that were predicted to alter sensitivity to neuraminidase inhibitors (NAIs) and/or receptor-binding specificity. We tested H5N1 viruses isolated from poultry and humans between 2004 and 2010 for sensitivity to the NAIs oseltamivir (Tamiflu) and zanamivir (Relenza). All viruses were sensitive to both inhibitors; however, we identified a virus with a mildly decreased sensitivity to zanamivir and have predicted that a V149A mutation is responsible. We also identified a virus with a hemagglutinin A134V mutation, present in a subpopulation amplified directly from a human sample. Using reverse genetics, we verified that this mutation is adaptative for human α2,6-linked sialidase receptors. The importance of an ongoing surveillance of H5N1 antigenic variance and genetic drift that may alter receptor binding and sensitivities of H5N1 viruses to NAIs cannot be underestimated while avian influenza remains a pandemic threat.

Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity

Nature ◽  
1983 ◽  
Vol 304 (5921) ◽  
pp. 76-78 ◽  
Author(s):  
G. N. Rogers ◽  
J. C. Paulson ◽  
R. S. Daniels ◽  
J. J. Skehel ◽  
I. A. Wilson ◽  
...  
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Binding Specificity ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Receptor Binding Specificity

Evidence that the alpha-subunit influences the specificity of receptor binding of the equine gonadotrophins

1997 ◽  
Vol 155 (2) ◽  
pp. 241-245 ◽  
Author(s):  
M Chopineau ◽  
N Martinat ◽  
H Marichatou ◽  
C Troispoux ◽  
C Auge-Gouillou ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Molecular Basis ◽  
Binding Specificity ◽  
Chorionic Gonadotrophin ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Beta Hcg ◽  
In Vitro Bioassays ◽  
Receptor Binding Specificity

Horse LH/chorionic gonadotrophin (eLH/CG) exhibits, in addition to its normal LH activity, a high FSH activity in all other species tested. Donkey LH/CG (dkLH/CG) also exhibits FSH activity in other species, but about ten times less than the horse hormone. In order to understand the molecular basis of these dual gonadotrophic activities of eLH/CG and dkLH/CG better, we expressed, in COS-7 cells, hybrids between horse and donkey subunits, between horse or donkey alpha-subunit and human CG beta (hCG beta), and also between the porcine alpha-subunit and horse or donkey LH/CG beta. The resultant recombinant hybrid hormones were measured using specific FSH and LH in vitro bioassays which give an accurate measure of receptor binding specificity and activation. Results showed that it is the beta-subunit that determines the level of FSH activity, in agreement with the belief that it is the beta-subunit which determines the specificity of action of the gonadotrophins. However, donkey LH/CG beta combined with a porcine alpha-subunit exhibited no FSH activity although it showed full LH activity. Moreover, the hybrid between horse or donkey alpha-subunit and hCG beta also exhibited only LH activity. Thus, the low FSH activity of dkLH/CG requires an equine (donkey or horse) alpha-subunit combined with dkLH/CG beta. These results provide the first evidence that an alpha-subunit can influence the specificity of action of a gonadotrophic hormone.

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