High specificity of a phosphate transport protein determined by hydrogen bonds

Nature ◽  
1990 ◽  
Vol 347 (6291) ◽  
pp. 402-406 ◽  
Author(s):  
Hartmut Luecke ◽  
Florante A. Quiocho
Keyword(s):  
Hydrogen Bonds ◽  
High Specificity ◽  
Phosphate Transport ◽  
Transport Protein

scholarly journals Molecular basis of flexible peptide recognition by an antibody

2020 ◽  
Vol 167 (4) ◽  
pp. 343-345
Author(s):  
Koki Makabe
Keyword(s):  
Hydrogen Bonds ◽  
High Specificity ◽  
Recognition Mechanism ◽  
Intramolecular Hydrogen Bonds ◽  
Peptide Recognition ◽  
X Ray Crystallography ◽  
Biophysical Techniques ◽  
Antibody Design ◽  
Dynamics Simulations ◽  
Intramolecular Hydrogen

Abstract Antibodies can recognize various types of antigens with high specificity and affinity and peptide is one of their major targets. Understanding an antibody’s molecular recognition mechanism for peptide is important for developing clones with a higher specificity and affinity. Here, the author reviews recent progresses in flexible peptide recognition by an antibody using several biophysical techniques, including X-ray crystallography, molecular dynamics simulations and calorimetric measurements. A set of two reports highlight the importance of intramolecular hydrogen bonds that form in an unbound flexible state. Such intramolecular hydrogen bonds restrict the fluctuation of the peptide and reduce the conformational entropy, resulting in the destabilization of the unbound state and increasing the binding affinity by increasing the free energy change. These detailed analyses will aid in the antibody design in the future.

scholarly journals Analysis of human hepatic microsomal glucose-6-phosphatase in clinical conditions where the T2 pyrophosphate/phosphate transport protein is absent

1992 ◽  
Vol 281 (3) ◽  
pp. 859-863 ◽  
Author(s):  
R C Nordlie ◽  
H M Scott ◽  
I D Waddell ◽  
R Hume ◽  
A Burchell
Keyword(s):  
Endoplasmic Reticulum ◽  
Transport System ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Hepatic Microsomes ◽  
Phosphatase System ◽  
Pyrophosphatase Activity ◽  
Protein Components ◽  
Clinical Conditions

The availability of a rare set of human hepatic microsomes in which T2, a pyrophosphate/phosphate transport protein of the glucose-6-phosphatase system, has been shown immunologically to be completely absent, has permitted further characterization of multicomponent glucose-6-phosphatase (EC 3.1.3.9). Pyrophosphatase activity in intact microsomes was found to be totally absent, but was normal in disrupted microsomes. However, Pi did not accumulate within the lumen of the microsomes when glucose 6-phosphate was the substrate. This was not as predicted if there is only one transport protein in the endoplasmic reticulum capable of transporting Pi, produced by glucose-6-phosphatase, out of the lumen. The results suggest that the pyrophosphate/phosphate transport system of human hepatic endoplasmic reticulum must be more complex than previously thought, as it must comprise at least two protein components.

Molecular Cloning of the cDNA Encoding a Human Renal Sodium Phosphate Transport Protein and Its Assignment to Chromosome 6p21.3-p23

Genomics ◽  
1993 ◽  
Vol 18 (2) ◽  
pp. 355-359 ◽  
Author(s):  
Samuel S. Chong ◽  
Kristleifur Kristjansson ◽  
Huda Y. Zoghbi ◽  
Mark R. Hughes
Keyword(s):  
Molecular Cloning ◽  
Sodium Phosphate ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Chromosome 6P21.3
Sign in / Sign up

Export Citation Format

Share Document