Immucillin-H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange

Protein Science

Volumn 9, Issue 9, 2000, Pages 1660-1668

  Wang, Fang ^a   Miles, Robert W ^a   Kicska, Gregory ^a   Nieves, Edward ^a   Schramm, Vern L ^a   Angeletti, Ruth Hogue ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

H D exchange; Immucillin H; Mass spectrometry; Negative cooperativity; One third the sites reactivity; Purine nucleoside phosphorylase

Indexed keywords

IMMUCILLIN H; PURINE NUCLEOSIDE PHOSPHORYLASE; PURINE NUCLEOSIDE PHOSPHORYLASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; AUTOIMMUNE DISEASE; CONFORMATIONAL TRANSITION; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME DEFICIENCY; ENZYME INHIBITION; ENZYME INHIBITOR COMPLEX; ENZYME SUBSTRATE; GRAFT VERSUS HOST REACTION; IMMUNE DEFICIENCY; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; T CELL LEUKEMIA;

EID: 0033819339     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.9.1660     Document Type: Article

References (27)

1. Contributions of mass spectrometry to peptide and protein structure
2. Purine nucleoside phosphorylase. 2. Catalytic mechanism
3. Synthesis of transition state inhibitors for N-riboside hydrolases and transferases
4. Transition state analogue inhibitors of protozoan nucleoside hydrolases
5. Immunodeficiency diseases caused by adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency
6. Mass spectrometric measurement of changes in protein hydrogen exchange rates that result from point mutation
7. Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin
8. Hydrogen/deuterium exchange electrospray ionization mass spectrometry: A method for probing protein conformational changes in solution
9. Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity
10. Purine nucleoside phosphorylase. Catalytic mechanism and transition state analysis of the arsenolysis reaction
11. Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution
12. Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
13. Identification of protein-protein interfaces by decreased amide proton solvent accessibility
14. Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues
15. One-third-the-sites transition state inhibitors for purine nucleoside phosphorylase
16. Inhibitors of the enzyme purine nucleoside phosphorylase
17. The behavior and significance of slow-binding enzyme inhibitors
18. Comparison of initial velocity and binding data for allosteric adenosine monophosphate nucleosidase
19. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
20. Amide hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of E. coli dihydropicolinate reductase
21. Conformation and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
22. 2+-induced conformation changes in the regulatory domain of human cardiac troponin C
23. Substrate binding and conformational changes of Clostridium glutamicum diaminopimelate dehydrogenase revealed by hydrogen/deuterium exchange and electrospray mass spectrometry
24. Advances in protein hydrogen exchange by mass spectrometry
25. FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR
26. Amide hydrogen exchange determined by mass spectrometry: Application to rabbit muscle aldolase
27. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation