An Intracellular Adenine Nucleotide Binding Site Inhibits Guanylyl Cyclase C by a Guanine Nucleotide-Dependent Mechanism†

Biochemistry ◽  
1996 ◽  
Vol 35 (10) ◽  
pp. 3213-3221 ◽  
Author(s):  
Scott J. Parkinson ◽  
Scott A. Waldman
Keyword(s):  
Binding Site ◽  
Guanylyl Cyclase ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Guanine Nucleotide ◽  
Guanylyl Cyclase C ◽  
Dependent Mechanism

Binding of the Fluorescein Derivative Eosin Y to the Mitochondrial ADP/ATP Carrier:  Characterization of the Adenine Nucleotide Binding Site†

Biochemistry ◽  
1998 ◽  
Vol 37 (1) ◽  
pp. 424-432 ◽  
Author(s):  
Eiji Majima ◽  
Nana Yamaguchi ◽  
Hiroshi Chuman ◽  
Yasuo Shinohara ◽  
Mayumi Ishida ◽  
...  
Keyword(s):  
Binding Site ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Eosin Y

scholarly journals Identification of an Adenine-Nucleotide-Binding Site on Interferon alpha2

1997 ◽  
Vol 247 (3) ◽  
pp. 762-769 ◽  
Author(s):  
Michael C. Olcott ◽  
Boyd E. Haley
Keyword(s):  
Binding Site ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site

scholarly journals 2.9 Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: Domain movements fragment the adenine nucleotide binding site

2008 ◽  
Vol 9 (2) ◽  
pp. 218-231 ◽  
Author(s):  
Valentin A. Ilyin ◽  
Brenda Temple ◽  
Mei Hu ◽  
Charles W. Carter ◽  
Genpei Li ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Trna Synthetase ◽  
Nucleotide Binding Site ◽  
Ligand Free

scholarly journals PROPERTIES OF THE PROTEIN SUBUNIT OF CENTRAL-PAIR AND OUTER-DOUBLET MICROTUBULES OF SEA URCHIN FLAGELLA

1968 ◽  
Vol 38 (2) ◽  
pp. 304-315 ◽  
Author(s):  
Michael L. Shelanski ◽  
Edwin W. Taylor
Keyword(s):  
Molecular Weight ◽  
Binding Site ◽  
Sea Urchin ◽  
Guanidine Hydrochloride ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Guanine Nucleotide ◽  
Protein Subunit ◽  
Central Pair ◽  
Guanine Nucleotide Binding

The subunit protein has been isolated from the central-pair and outer-doublet microtubules of sea urchin sperm tails. Both proteins have a sedimentation constant of 6S and a molecular weight of 120,000. Both are converted to a 60,000 molecular weight species by denaturation in 6 M guanidine hydrochloride and reduction with mercaptoethanol. The reduced-alkylated proteins have the same Rf on disc electrophoresis, and the same amino acid composition, which is very similar to that of muscle actin. The central-pair protein has one binding site for colchicine per 120,000 g. Both proteins appear to have a guanine nucleotide binding site, but the ability to bind GTP in solution has been demonstrated only for the central-pair protein. Although 1 mole of guanine nucleotide is bound per 60,000 g to outer-doublet tubules, the protein obtained by dissolving the doublets at pH 10.5 has lost the guanine nucleotide-binding site and also shows little or no colchicine-binding activity. Comparison of the properties of the isolated protein with electron microscopic evidence on structure of microtubules suggests that the chemical subunit (M = 120,000) consists of two of the 40 A morphological subunits.

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