scholarly journals Characterization of the Hypoxia-inducible Protein Binding Site within the Pyrimidine-rich Tract in the 3′-Untranslated Region of the Tyrosine Hydroxylase mRNA

1996 ◽  
Vol 271 (6) ◽  
pp. 3293-3299 ◽  
Author(s):  
Maria F. Czyzyk-Krzeska ◽  
John E. Beresh
Keyword(s):  
Tyrosine Hydroxylase ◽  
Protein Binding ◽  
Binding Site ◽  
Untranslated Region ◽  
Protein Binding Site ◽  
Inducible Protein

scholarly journals Organization of the 3′-boundary of the chicken α globin gene domain and characterization of a CR 1-specific protein binding site

1990 ◽  
Vol 18 (3) ◽  
pp. 401-409 ◽  
Author(s):  
Gabriel Farache ◽  
Sergey V. Razin ◽  
Félix Recillas Targa ◽  
Klaus Scherrer
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Globin Gene ◽  
Specific Protein ◽  
Protein Binding Site ◽  
Globin Gene Domain

scholarly journals An NMR characterization of the regA protein-binding site of bacteriophage T4 gene 44 mRNA.

1991 ◽  
Vol 266 (27) ◽  
pp. 17832-17837
Author(s):  
A.A. Szewczak ◽  
K.R. Webster ◽  
E.K. Spicer ◽  
P.B. Moore
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Bacteriophage T4 ◽  
Protein Binding Site ◽  
Nmr Characterization

106 Severe helical distortion of the U1A mRNA 3′ untranslated region induced by the U1A protein binding site

1997 ◽  
Vol 25 (4) ◽  
pp. S641-S641
Author(s):  
Richard J. Grainger ◽  
Alastair I. H. Murchie ◽  
David M. J. Lilley
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Untranslated Region ◽  
Protein Binding Site ◽  
U1a Protein

scholarly journals Characterization of the S100A1 Protein Binding Site on TRPC6 C-Terminus

PLoS ONE ◽  
2013 ◽  
Vol 8 (5) ◽  
pp. e62677 ◽  
Author(s):  
Jan Bily ◽  
Lenka Grycova ◽  
Blanka Holendova ◽  
Michaela Jirku ◽  
Hana Janouskova ◽  
...  
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Protein Binding Site ◽  
C Terminus

scholarly journals Functional homology between the yeast regulatory proteins GAL4 and LAC9: LAC9-mediated transcriptional activation in Kluyveromyces lactis involves protein binding to a regulatory sequence homologous to the GAL4 protein-binding site.

1987 ◽  
Vol 7 (12) ◽  
pp. 4400-4406 ◽  
Author(s):  
K D Breunig ◽  
P Kuger
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Transcriptional Activation ◽  
Kluyveromyces Lactis ◽  
Regulatory Protein ◽  
Binding Activity ◽  
Protein Binding Site ◽  
Regulatory Sequence ◽  
Functional Homology ◽  
Beta Galactosidase

As shown previously, the beta-galactosidase gene of Kluyveromyces lactis is transcriptionally regulated via an upstream activation site (UASL) which contains a sequence homologous to the GAL4 protein-binding site in Saccharomyces cerevisiae (M. Ruzzi, K.D. Breunig, A.G. Ficca, and C.P. Hollenberg, Mol. Cell. Biol. 7:991-997, 1987). Here we demonstrate that the region of homology specifically binds a K. lactis regulatory protein. The binding activity was detectable in protein extracts from wild-type cells enriched for DNA-binding proteins by heparin affinity chromatography. These extracts could be used directly for DNase I and exonuclease III protection experiments. A lac9 deletion strain, which fails to induce the beta-galactosidase gene, did not contain the binding factor. The homology of LAC9 protein with GAL4 (J.M. Salmeron and S. A. Johnston, Nucleic Acids Res. 14:7767-7781, 1986) strongly suggests that LAC9 protein binds directly to UASL and plays a role similar to that of GAL4 in regulating transcription.

scholarly journals Valine-279 Deletion–Mutation on Arginine Vasopressin Receptor 2 Causes Obstruction in G-Protein Binding Site: A Clinical Nephrogenic Diabetes Insipidus Case and Its Sub-Molecular Pathogenic Analysis

Biomedicines ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 301
Author(s):  
Ming-Chun Chen ◽  
Yu-Chao Hsiao ◽  
Chun-Chun Chang ◽  
Sheng-Feng Pan ◽  
Chih-Wen Peng ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Protein Binding ◽  
Diabetes Insipidus ◽  
Binding Site ◽  
G Protein ◽  
Arginine Vasopressin ◽  
Nephrogenic Diabetes Insipidus ◽  
Md Simulations ◽  
Protein Binding Site ◽  
Vasopressin Receptor

Congenital nephrogenic diabetes insipidus (CNDI) is a genetic disorder caused by mutations in arginine vasopressin receptor 2 (AVPR2) or aquaporin 2 genes, rendering collecting duct cells insensitive to the peptide hormone arginine vasopressin stimulation for water reabsorption. This study reports a first identified AVPR2 mutation in Taiwan and demonstrates our effort to understand the pathogenesis caused by applying computational structural analysis tools. The CNDI condition of an 8-month-old male patient was confirmed according to symptoms, family history, and DNA sequence analysis. The patient was identified to have a valine 279 deletion–mutation in the AVPR2 gene. Cellular experiments using mutant protein transfected cells revealed that mutated AVPR2 is expressed successfully in cells and localized on cell surfaces. We further analyzed the pathogenesis of the mutation at sub-molecular levels via long-term molecular dynamics (MD) simulations and structural analysis. The MD simulations showed while the structure of the extracellular ligand-binding domain remains unchanged, the mutation alters the direction of dynamic motion of AVPR2 transmembrane helix 6 toward the center of the G-protein binding site, obstructing the binding of G-protein, thus likely disabling downstream signaling. This study demonstrated that the computational approaches can be powerful tools for obtaining valuable information on the pathogenesis induced by mutations in G-protein-coupled receptors. These methods can also be helpful in providing clues on potential therapeutic strategies for CNDI.

Sign in / Sign up

Export Citation Format

Share Document