Structural characterization of two alternate conformations in a calbindin D9k-based molecular switch

Biochemistry

Volumn 50, Issue 25, 2011, Pages 5583-5589

  Stratton, Margaret M ^a   McClendon, Sebastian ^b   Eliezer, David ^b   Loh, Stewart N ^a  

^a State University of New York Upstate Medical University: College of Medicine   (United States)

^b WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CALBINDIN; CONFORMATIONAL CHANGE; DISORDERED REGIONS; FOLDING REACTIONS; INTERCONVERSIONS; MOLECULAR SWITCHES; PARAMAGNETIC RELAXATION ENHANCEMENTS; RESONANCE ASSIGNMENTS; STRUCTURAL CHARACTERIZATION; STRUCTURAL EVIDENCE; WILD TYPES;

AMINO ACIDS; CALCIUM; PARAMAGNETISM; PROTEINS; RESONANCE;

CONFORMATIONS;

CALBINDIN; CALCIUM; CALCIUM SENSING RECEPTOR;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; MUTATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE;

BIOSENSING TECHNIQUES; CALCIUM-BINDING PROTEIN, VITAMIN D-DEPENDENT; LIGANDS; MOLECULAR PROBES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING;

EID: 79959444804     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi102040g     Document Type: Article

References (15)

1. 2+-sensing molecular switch based on alternate frame protein folding ACS Chem. Biol. 3, 723-732
2. Stratton, M. M. and Loh, S. N. (2010) On the mechanism of protein fold-switching by a molecular sensor Proteins: Struct., Funct., Bioinf. 78, 3260-3269
3. Mitrea, D. M., Parsons, L., and Loh, S. N. (2010) Engineering an artificial zymogen by alternate frame protein folding Proc. Natl. Acad. Sci. U.S.A. 107, 2824-2829
4. 2+ binding J. Mol. Biol. 231, 415-430 (Pubitemid 23188262)
5. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
6. Johnson, B. and Blevins, R. (1994) NMRView: A computer program for the visualization and analysis of NMR data J. Biomol. NMR 4, 603-614
7. Wishart, D. S. and Sykes, B. D. (1994) Chemical shifts as a tool for structure determination Methods Enzymol. 239, 363-392
8. 9k P43G Biomol. NMR Assignments 5, 79-84
9. 9k EF-hands Proteins 47, 323-333 (Pubitemid 34438682)
10. Eliezer, D. (2006) Characterizing residual structure in disordered protein states using NMR Methods Mol. Biol. 350, 49-68
11. Eliezer, D. (2009) Biophysical characterization of intrinsically disordered proteins Curr. Opin. Struct. Biol. 19, 23-30
12. Dunker, A. K., Silman, I., Uversky, V. N., and Sussman, J. L. (2008) Function and structure of inherently disordered proteins Curr. Opin. Struct. Biol. 18, 756-764
13. Wright, P. E. and Dyson, H. J. (2009) Linking folding and binding Curr. Opin. Struct. Biol. 19, 31-38
14. Galea, C. A., Pagala, V. R., Obenauer, J. C., Park, C. G., Slaughter, C. A., and Kriwacki, R. W. (2006) Proteomic studies of the intrinsically unstructured mammalian proteome J. Proteome Res. 5, 2839-2848 (Pubitemid 44595184)
15. Uversky, V. N. and Dunker, A. K. (2010) Understanding protein non-folding Biochim. Biophys. Acta 1804, 1231-1264