The Proton Relaxation Enhancement Properties of Concanavalin A

作者: Brian H Barber , Jeremy P Carver , None

DOI: 10.1016/S0021-9258(19)44047-7

关键词: Relaxation (NMR)ProtonCrystallographyKinetic energyChemistryCrystal structureStereochemistryMoleculeConcanavalin AFolding (chemistry)Binding site

摘要: Abstract The measurement of the proton relaxation rate (1/T1) enhancement (e1*) for concanavalin A (Con A)-Mn2+ complex as a function time following addition Mn2+ indicates pH-dependent structural rearrangement at bound site. excess Ca2+ interrupts this kinetic process and results in reduced time-independent value e1*. further α-methyl-d-glucoside to Con A-Mn2+-Ca2+ also alters observable Using recently published 2 resolution crystal structure A, are interpreted arising from gradual folding loop residues 12 22 over initial binding site (formed by 8, 10, 24) close off free access water molecules.

参考文章(16)
George H. Reed, Mildred Cohn, Electron Paramagnetic Resonance Spectra of Manganese(II)-Protein Complexes MANGANESE(II)-CONCANAVALIN A Journal of Biological Chemistry. ,vol. 245, pp. 662- 664 ,(1970) , 10.1016/S0021-9258(18)63380-0
James B. Sumner, Stacey F. Howell, Identification of Hemagglutinin of Jack Bean with Concanavalin A. Journal of Bacteriology. ,vol. 32, pp. 227- 237 ,(1936) , 10.1128/JB.32.2.227-237.1936
B.B.L. Agrawal, I.J. Goldstein, Protein-Carbohydrate interaction Archives of Biochemistry and Biophysics. ,vol. 124, pp. 218- 229 ,(1968) , 10.1016/0003-9861(68)90322-6
W. Eckhart, R. Dulbecco, M. M. Burger, Temperature-Dependent Surface Changes in Cells Infected or Transformed by a Thermosensitive Mutant of Polyoma Virus Proceedings of the National Academy of Sciences of the United States of America. ,vol. 68, pp. 283- 286 ,(1971) , 10.1073/PNAS.68.2.283
KARL D. HARDMAN, CLINTON F. AINSWORTH, Myo-inositol binding site of concanavalin A. Nature. ,vol. 237, pp. 54- 55 ,(1972) , 10.1038/NEWBIO237054A0
A. Joseph Kalb, Ariel Lustig, The molecular weight of concanavalin A Biochimica et Biophysica Acta (BBA) - Protein Structure. ,vol. 168, pp. 366- 367 ,(1968) , 10.1016/0005-2795(68)90161-X
G. M. Edelman, B. A. Cunningham, G. N. Reeke, J. W. Becker, M. J. Waxdal, J. L. Wang, The Covalent and Three-Dimensional Structure of Concanavalin A Proceedings of the National Academy of Sciences of the United States of America. ,vol. 69, pp. 2580- 2584 ,(1972) , 10.1073/PNAS.69.9.2580
Hannah Ben-Bassat, Michael Inbar, Leo Sachs, Changes in the structural organization of the surface membrane in malignant cell transformation. The Journal of Membrane Biology. ,vol. 6, pp. 183- 194 ,(1971) , 10.1007/BF01872276