The Three-Dimensional Structure of the N-Terminal Domain of Corticotropin-Releasing Factor Receptors: Sushi Domains and the B1 Family of G Protein-Coupled Receptors

2006 ◽  
Vol 1070 (1) ◽  
pp. 105-119 ◽  
Author(s):  
M. H. PERRIN
Keyword(s):  
G Protein ◽  
Three Dimensional ◽  
G Protein Coupled Receptors ◽  
Corticotropin Releasing Factor ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Terminal Domain ◽  
G Protein Coupled

scholarly journals Advances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, a Model of G-Protein-Coupled Receptors (GPCRs)†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (26) ◽  
pp. 7761-7772 ◽  
Author(s):  
David C. Teller ◽  
Tetsuji Okada ◽  
Craig A. Behnke ◽  
Krzysztof Palczewski ◽  
Ronald E. Stenkamp
Keyword(s):  
High Resolution ◽  
G Protein ◽  
Three Dimensional ◽  
G Protein Coupled Receptors ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
G Protein Coupled

Demystifying the three dimensional structure of G protein-coupled receptors (GPCRs) with the aid of molecular modeling

2003 ◽  
pp. 2949 ◽  
Author(s):  
Stefano Moro ◽  
Francesca Deflorian ◽  
Giampiero Spalluto ◽  
Giorgia Pastorin ◽  
Barbara Cacciari ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
G Protein ◽  
Three Dimensional ◽  
G Protein Coupled Receptors ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
G Protein Coupled

Three-Dimensional Structure of the Highly Conserved Seventh Transmembrane Domain of G-Protein-Coupled Receptors

1994 ◽  
Vol 225 (3) ◽  
pp. 827-843 ◽  
Author(s):  
Jean-Philippe Berlose ◽  
Odile Convert ◽  
Alie Brunissen ◽  
Gerard Chassaing ◽  
Solange Lavielle
Keyword(s):  
G Protein ◽  
Transmembrane Domain ◽  
Three Dimensional ◽  
G Protein Coupled Receptors ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
G Protein Coupled

Modulation of proteostasis and protein trafficking: a therapeutic avenue for misfolded G protein-coupled receptors causing disease in humans

2019 ◽  
Vol 3 (1) ◽  
pp. 39-52
Author(s):  
Alfredo Ulloa-Aguirre ◽  
Jo Ann Janovick
Keyword(s):  
G Protein ◽  
Protein Trafficking ◽  
Protein Misfolding ◽  
Hypogonadotropic Hypogonadism ◽  
Three Dimensional ◽  
G Protein Coupled Receptors ◽  
Dimensional Structure ◽  
Stable Conformation ◽  
Mutant Proteins ◽  
G Protein Coupled

Abstract Proteostasis refers to the process whereby the cell maintains in equilibrium the protein content of different compartments. This system consists of a highly interconnected network intended to efficiently regulate the synthesis, folding, trafficking, and degradation of newly synthesized proteins. Molecular chaperones are key players of the proteostasis network. These proteins assist in the assembly and folding processes of newly synthesized proteins in a concerted manner to achieve a three-dimensional structure compatible with export from the endoplasmic reticulum to other cell compartments. Pharmacologic interventions intended to modulate the proteostasis network and tackle the devastating effects of conformational diseases caused by protein misfolding are under development. These include small molecules called pharmacoperones, which are highly specific toward the target protein serving as a molecular framework to cause misfolded mutant proteins to fold and adopt a stable conformation suitable for passing the scrutiny of the quality control system and reach its correct location within the cell. Here, we review the main components of the proteostasis network and how pharmacoperones may be employed to correct misfolding of two G protein-coupled receptors, the vasopressin 2 receptor and the gonadotropin-releasing hormone receptor, whose mutations lead to X-linked nephrogenic diabetes insipidus and congenital hypogonadotropic hypogonadism in humans respectively.

The dark and bright sides of an enzyme: a three dimensional structure of the N-terminal domain of Zophobas morio luciferase-like enzyme, inferences on the biological function and origin of oxygenase/luciferase activity

2016 ◽  
Vol 15 (5) ◽  
pp. 654-665 ◽  
Author(s):  
R. A. Prado ◽  
C. R. Santos ◽  
D. I. Kato ◽  
M. T. Murakami ◽  
V. R. Viviani
Keyword(s):  
Biological Function ◽  
Luciferase Activity ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Catalytic Residue ◽  
Three Dimensional Structure ◽  
Catalytic Activities ◽  
Terminal Domain ◽  
Coa Ligase

The structure and catalytic activities of a Malpighian luciferase-like enzyme indicate a generalistic xenobiotic CoA-ligase and a catalytic residue for bioluminescence.

scholarly journals Identification of a Novel Family of Targets of PYK2 Related to Drosophila Retinal Degeneration B (rdgB) Protein

1999 ◽  
Vol 19 (3) ◽  
pp. 2278-2288 ◽  
Author(s):  
Sima Lev ◽  
John Hernandez ◽  
Ricardo Martinez ◽  
Alon Chen ◽  
Greg Plowman ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Retinal Degeneration ◽  
G Protein ◽  
Binding Proteins ◽  
G Protein Coupled Receptors ◽  
Sequence Motif ◽  
Phosphoinositide Metabolism ◽  
Amino Terminal ◽  
Terminal Domain ◽  
G Protein Coupled

ABSTRACT The protein tyrosine kinase PYK2 has been implicated in signaling pathways activated by G-protein-coupled receptors, intracellular calcium, and stress signals. Here we describe the molecular cloning and characterization of a novel family of PYK2-binding proteins designated Nirs (PYK2 N-terminal domain-interacting receptors). The three Nir proteins (Nir1, Nir2, and Nir3) bind to the amino-terminal domain of PYK2 via a conserved sequence motif located in the carboxy terminus. The primary structures of Nirs reveal six putative transmembrane domains, a region homologous to phosphatidylinositol (PI) transfer protein, and an acidic domain. The Nir proteins are the human homologues of the Drosophila retinal degeneration B protein (rdgB), a protein implicated in the visual transduction pathway in flies. We demonstrate that Nirs are calcium-binding proteins that exhibit PI transfer activity in vivo. Activation of PYK2 by agents that elevate intracellular calcium or by phorbol ester induce tyrosine phosphorylation of Nirs. Moreover, PYK2 and Nirs exhibit similar expression patterns in several regions of the brain and retina. In addition, PYK2-Nir complexes are detected in lysates prepared from cultured cells or from brain tissues. Finally, the Nir1-encoding gene is located at human chromosome 17p13.1, in proximity to a locus responsible for several human retinal diseases. We propose that the Nir and rdgB proteins represent a new family of evolutionarily conserved PYK2-binding proteins that play a role in the control of calcium and phosphoinositide metabolism downstream of G-protein-coupled receptors.

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