Importance of the Extracellular Domain for Prostaglandin EP2 Receptor Function

1999 ◽  
Vol 56 (3) ◽  
pp. 545-551 ◽  
Author(s):  
Brett A. Stillman ◽  
Matthew D. Breyer ◽  
Richard M. Breyer
Keyword(s):  
Extracellular Domain ◽  
Receptor Function ◽  
Ep2 Receptor

Many Proline Residues in the Extracellular Domain Contribute to Glycine Receptor Function

2020 ◽  
Vol 11 (17) ◽  
pp. 2658-2665
Author(s):  
Merryn E. Hughes ◽  
Susanne M. Mesoy ◽  
Emily Capes ◽  
Sarah C. R. Lummis
Keyword(s):  
Glycine Receptor ◽  
Extracellular Domain ◽  
Receptor Function

Exchange of W39 by A within the N-terminal extracellular domain of the GLP-1 receptor results in a loss of receptor function

Peptides ◽  
1996 ◽  
Vol 17 (4) ◽  
pp. 565-570 ◽  
Author(s):  
Brigitte Van Eyll ◽  
Burkhard Göke ◽  
Andreas Wilmen ◽  
Rüdiger Göke
Keyword(s):  
Extracellular Domain ◽  
Receptor Function

scholarly journals Entry of Amphotropic Murine Leukemia Virus Is Influenced by Residues in the Putative Second Extracellular Domain of Its Receptor, Pit2

1998 ◽  
Vol 72 (6) ◽  
pp. 4956-4961 ◽  
Author(s):  
Betsy D. Leverett ◽  
Karen B. Farrell ◽  
Maribeth V. Eiden ◽  
Carolyn A. Wilson
Keyword(s):  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Critical Role ◽  
Functional Characterization ◽  
Extracellular Domain ◽  
Receptor Function ◽  
Amphotropic Murine Leukemia Virus ◽  
Fold Reduction ◽  
Gibbon Ape Leukemia Virus ◽  
Murine Leukemia

ABSTRACT Human cells express distinct but related receptors for the gibbon ape leukemia virus (GALV) and the amphotropic murine leukemia virus (A-MuLV), termed Pit1 and Pit2, respectively. Pit1 is not able to function as a receptor for A-MuLV infection, while Pit2 does not confer susceptibility to GALV. Previous studies of chimeric receptors constructed by interchanging regions of Pit1 and Pit2 failed to clarify the determinants unique to Pit2 which correlate with A-MuLV receptor function. In order to identify which regions of Pit2 are involved in A-MuLV receptor function, we exchanged the putative second and third extracellular domains of Pit1, either individually or together, with the corresponding regions of Pit2. Our functional characterization of these receptors indicates a role for the putative second extracellular domain (domain II) in A-MuLV infection. We further investigated the influence of domain II with respect to A-MuLV receptor function by performing site-specific mutagenesis within this region of Pit2. Many of the mutations had little or no effect on receptor function. However, the substitution of serine for methionine at position 138 (S138M) in a Pit1 chimera containing domain II of Pit2 resulted in a 1,000-fold reduction in A-MuLV receptor function. Additional mutations made within domain II of the nonfunctional S138M mutant restored receptor function to nearly wild-type efficiency. The high degree of tolerance for mutations as well as the compensatory effect of particular substitutions observed within domain II suggests that an element of secondary structure within this region plays a critical role in the interaction of the receptor with A-MuLV.

Sign in / Sign up

Export Citation Format

Share Document