Disulfide bond plasticity in epidermal growth factor

Proteins: Structure, Function and Genetics

Volumn 40, Issue 1, 2000, Pages 168-174

  Sampoli Benitez, Benedetta A ^a   Komives, Elizabeth A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Cysteine disulfide isomer; NMR solution structure

Indexed keywords

EPIDERMAL GROWTH FACTOR;

ARTICLE; CALCULATION; CONTROLLED STUDY; DISULFIDE BOND; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; COMPUTER SIMULATION; DISULFIDES; EPIDERMAL GROWTH FACTOR; ISOMERISM; MICE; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY;

MURINAE;

EID: 0008948589     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000701)40:1<168::AID-PROT180>3.0.CO;2-N     Document Type: Article

References (18)

1. Montelione GT, Wuthrich K, Burgess AW, et al. Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints. Biochemistry 1992;31:236-249.
2. Tejero R, Bassolino-Klimas D, Bruccoleri RE, Montelione GT. Simulated annealing with restrained molecular dynamics using CONGEN: energy refinement of the NMR solution structures of epidermal and type-alpha transforming growth factors. Protein Sci 1996;5:578-592.
3. Li YC, Montelione GT. Human type-alpha transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements. Biochemistry 1995;34:2408-2423.
4. Chang JY, Schindler P, Ramseier U, Lai PH. The disulfide folding pathway of human epidermal growth factor. J Biol Chem 1995;270: 9207-9216.
5. Weissman JS, Kim PS. Reexamination of the folding of BPTI. Predominance of native intermediates. Science 1991;253;1386-1393.
6. Zhu H, Dupureur CM, Zhang X, Tsai MD. Phospholipase A2 engineering. The roles of disulfide bonds in structure, conformational stability, and catalytic function. Biochemistry 1995;34: 15307-15314.
7. Tou JS, McGrath MF, Zupec ME, et al. Chemical synthesis of bovine transforming growth factor-α: synthesis, characterization and biological activity. Biochem Biophys Res Commun 1990;167: 484-491.
8. Violand BN, Tou JS, Vineyard BD, et al. Determination of the disulfide bond pairings in bovine transforming growth factor-α. Int J Peptide Protein Res 1991;37:463-467.
9. Groenen LC, Nice EC, Burgess AW. Structure-function relationships for the EGF/TGFα family of mitogens. Growth Factors 1994;11:235-257.
10. Hunter MJ, Komives EA. Thrombin-binding affinities of different disulfide-bonding isomers of the fifth EGF-like domain of thrombomodulin. Protein Sci 1995;4:2129-2137.
11. White CE, Hunter MJ, Meininger DP, White LR, Komives EA. The fifth EGF-like domain of thrombomodulin does not have an EGF-like disulfide bonding pattern. Proc Natl Acad Sci USA 1996;93:10177-10182.
12. Sampoli Benitez BA, Hunter MJ, Meininger DP, Komives EA Structure of the fifth EGF-like domain of thrombomodulin: an EGF-like domain with a novel disulfide-bonding pattern. J Mol Biol 1997;273:913-926.
13. Havel TF. An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Prog Biophys Mol Biol 1991;56:43-78.
14. Brünger AT. 1988. X-PLOR Version 3.1. A system for X-ray crystallography and NMR. New Haven: Yale University Press.
15. Diamond R. 1992. On the multiple simultaneous superimposition of molecular structures by rigid body transformations. Protein Sci 1:1279-1287
16. Laskowski RA, MacArthur MW, Moss DS, Thorton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993;26:283-291.
17. Salem GM, Hutchinson EG, Orengo CA, Thornton JM. Correlation of observed fold frequency with the occurrence of local structural motifs. J Mol Biol 1999;287:969-981.
18. Campbell ID, Bork P. Epidermal growth factor-like modules. Curr Opin Struct Biol 1993;3:385-392.