Molecular Symmetry as an Aid to Geometry Determination in Ligand Protein Complexes

Journal of Magnetic Resonance

Volumn 142, Issue 1, 2000, Pages 153-158

  Al Hashimi, H M ^a,b   Bolon, P J ^a   Prestegard, J H ^a  

^a UNIVERSITY OF GEORGIA   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

Homomultimer; Ligand bound geometry; Mannose binding protein; Order tensors; Symmetry

Indexed keywords

TRIXIS;

CARRIER PROTEIN; COLLECTIN; LECTIN; METHYL MANNOSIDE; METHYLMANNOSIDE;

ARTICLE; CHEMISTRY; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING;

CARRIER PROTEINS; COLLECTINS; LECTINS; MAGNETIC RESONANCE SPECTROSCOPY; METHYLMANNOSIDES; PROTEIN BINDING;

EID: 0033631450     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1999.1937     Document Type: Article

References (17)

1. J. R. Tolman, J. M. Flanagan, M. A. Kenedy, and J. H. Prestegard, Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution, Proc. Natl. Acad. Sci. USA 92, 9297-9283 (1995).
2. J. H. Prestegard, J. R. Tolman, H. M. Al-Hashimi, and M. Andrec, Protein structure and dynamics from field induced residual dipolar couplings, in "Modern Techniques in Protein NMR" (N. R. Krishna and L. J. Berliner, Eds.), pp. 311-355, Plenum, New York (1998).
3. N. Tjandra and A. Bax, Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium, Science 278, 1111-1114 (1997).
4. 13C couplings in the structure determination of magnetically oriented macromolecules in solution, Nature Struct. Biol. 4, 732-738 (1997).
5. M. R. Hansen, L. Mueller, and A. Pardi, Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions, Nature Struct. Biol. 5, 1065-1074 (1998).
6. J. H. Prestegard, New techniques in structural NMR - Anisotropic interactions. Nature Struct. Biol. 5, 517-522 (1998).
7. A. Saupe, Recent results in the field of liquid crystals, Angew. Chem., Int. Ed. Engl. 7, 97 (1968).
8. J. A. Losonczi and J. H. Prestegard, Nuclear magnetic resonance characterization of the myristoylated, N-terminal fragment of ADP-ribosylation factor 1 in a magnetically oriented membrane array, Biochemistry 37, 706-716 (1998).
9. M. W. F. Fischer, J. A. Losonczi, J. L. Weaver, and J. H. Prestegard, Domain orientation and dynamics in multi-domain proteins from residual dipolar couplings, Biochemistry 38, 9013-9022 (1999).
10. P. J. Bolon, H. M. Al-Hashimi, and J. H. Prestegard, Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex, J. Mol. Biol. 293, 107-115 (1999).
11. V. Dötsch and G. Wagner, New approaches to structure determination by NMR spectroscopy, Current Opin. Struct. Biol. 8, 619-623 (1998).
12. D. M. Brink and G. R. Satchler, "Angular Momentum," Clarendon Press, Oxford (1993).
13. 1H NMR, J. Carbohydrate Chem. 13, 513-543 (1994).
14. J. A. Losonczi, M. Andrec, M. W. F. Fischer, and J. H. Prestegard, Order matrix analysis of residual dipolar couplings using singular value decomposition, J. Magn. Reson. 138, 334-342 (1999).
15. H. J. Gabius, Animal lectins, Eur. J. Biochem. 243, 543-547 (1997).
16. M. Mammen, S. K. Choi, and G. M. Whitesides, Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors, Angew. Chem., Int. Ed. Engl. 37, 2755-2794 (1998).
17. M. Andrec and J. H. Prestegard, A metropolis Monte Carlo implementation of Bayesian time-domain parameter estimation: Application to coupling constant estimation from antiphase multiplets, J. Magn. Reson. 130, 217-232 (1998).