scholarly journals Identification by Site-directed Mutagenesis of Residues Involved in Ligand Recognition and Activation of the Human A3Adenosine Receptor

2002 ◽  
Vol 277 (21) ◽  
pp. 19056-19063 ◽  
Author(s):  
Zhan-Guo Gao ◽  
Aishe Chen ◽  
Dov Barak ◽  
Soo-Kyung Kim ◽  
Christa E. Müller ◽  
...  
Keyword(s):  
Site Directed Mutagenesis ◽  
Ligand Recognition ◽  
Directed Mutagenesis

scholarly journals Site-directed Mutagenesis Identifies Residues Involved in Ligand Recognition in the Human A2aAdenosine Receptor

1995 ◽  
Vol 270 (23) ◽  
pp. 13987-13997 ◽  
Author(s):  
Jeongho Kim ◽  
Jürgen Wess ◽  
A. Michiel van Rhee ◽  
Torsten Schöneberg ◽  
Kenneth A. Jacobson
Keyword(s):  
Site Directed Mutagenesis ◽  
Ligand Recognition ◽  
Directed Mutagenesis

Identification of Critical Residues for Ligand Binding in the Integrin β3 I-domain by Site-directed Mutagenesis

2002 ◽  
Vol 87 (04) ◽  
pp. 756-762 ◽  
Author(s):  
Jun Yamanouchi ◽  
Tatsushiro Tamura ◽  
Shigeru Fujita ◽  
Takaaki Hato
Keyword(s):  
Ligand Binding ◽  
Site Directed Mutagenesis ◽  
Structural Basis ◽  
Ligand Recognition ◽  
Directed Mutagenesis ◽  
Different Types ◽  
Β3 Integrin ◽  
Critical Residues ◽  
Α Subunits ◽  
Putative Ligand Binding

SummaryTo define the structural basis of ligand recognition by αIIb β3, we conducted site-directed mutagenesis of residues located on the top surface of the β3 I-domain that is homologous to the I-domain of several α subunits and contains a putative ligand binding site. Here we identify D158 and N215 in β3 as novel residues critical for ligand binding. Alanine substitution of D158 or N215 abolished binding of a ligand-mimetic antibody and fibrinogen to αIIb β3 induced by different types of integrin activation. CHO cells expressing recombinant αIIb β3 bearing D158A or N215A mutation did not adhere to fibrinogen. These mutations had the same effect on ligand binding to another β3 integrin, αV β3. Compared to the αI-domain structure, the βB-βC loop containing D158 in the β3 I-domain is quite different in length and sequence. These results suggest that the structure for ligand recognition is different in the βI- and αI-domains.

scholarly journals Molecular determinants for agonist recognition and discrimination in P2X2 receptors

2019 ◽  
Vol 151 (7) ◽  
pp. 898-911 ◽  
Author(s):  
Federica Gasparri ◽  
Jesper Wengel ◽  
Thomas Grutter ◽  
Stephan A. Pless
Keyword(s):  
Drug Targets ◽  
P2x Receptors ◽  
Carbonyl Oxygen ◽  
Site Directed Mutagenesis ◽  
Side Chain ◽  
Ligand Recognition ◽  
Directed Mutagenesis ◽  
Backbone Carbonyl ◽  
Molecular Determinants ◽  
Atp Analogues

P2X receptors (P2XRs) are trimeric ligand-gated ion channels that open a cation-selective pore in response to ATP binding. P2XRs contribute to synaptic transmission and are involved in pain and inflammation, thus representing valuable drug targets. Recent crystal structures have confirmed the findings of previous studies with regards to the amino acid chains involved in ligand recognition, but they have also suggested that backbone carbonyl atoms contribute to ATP recognition and discrimination. Here we use a combination of site-directed mutagenesis, amide-to-ester substitutions, and a range of ATP analogues with subtle alterations to either base or sugar component to investigate the contributions of backbone carbonyl atoms toward ligand recognition and discrimination in rat P2X2Rs. Our findings demonstrate that while the Lys69 backbone carbonyl makes an important contribution to ligand recognition, the discrimination between different ligands is mediated by both the side chain and the backbone carbonyl oxygen of Thr184. Together, our data demonstrate how conserved elements in P2X2Rs recognize and discriminate agonists.

The site-directed mutagenesis and prokaryotic expression of midkine gene in Cynoglossus semilaevis

2013 ◽  
Vol 37 (3) ◽  
pp. 330
Author(s):  
Yanan WANG ◽  
Xudong LIU ◽  
Linlin MU ◽  
Zhipeng LIU ◽  
Chunmei LI ◽  
...  
Keyword(s):  
Prokaryotic Expression ◽  
Cynoglossus Semilaevis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Site-directed mutagenesis on alkaline phosphatasefrompseudomonas aeruginosapao1 for enhanced activity

2016 ◽  
Vol 7 (4) ◽  
Author(s):  
UMA SELVARAJ ◽  
THIRUMALAI MUTHUKUMARESAN ◽  
GAYATHRI VIJAYENDRAN ◽  
SENTHIL KUMAR DEVAN ◽  
VENU BABU P ◽  
...  
Keyword(s):  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Enhanced Activity
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