The three-dimensional structure of a helix-less variant of intestinal fatty acid-binding protein

Protein Science

Volumn 7, Issue 6, 1998, Pages 1332-1339

  Steele, Ruth A ^a   Emmert, Daniel A ^a   Kao, Jeff ^a   Hodsdon, Michael E ^a   Frieden, Carl ^a   Cistola, David P ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Intestinal fatty acid binding protein; NMR spectroscopy; Protein structure

Indexed keywords

FATTY ACID; FATTY ACID BINDING PROTEIN; GLYCINE; PALMITIC ACID; SERINE;

ANIMAL TISSUE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; INTESTINE; LIGAND BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; RAT;

ANIMALIA;

EID: 0031776786     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070609     Document Type: Article

References (23)

1. Banaszak L, Winter N, Xu Z, Bernlohr DA, Cowan S, Jones TA. 1994. Lipid-binding proteins: A family of fatty acid and retinoid transport proteins. Adv Protein Chem 45:89-151.
2. Cistola DP, Kim K, Rogl H, Frieden C. 1996. Fatty acid interactions with a helix-less variant of intestinal fatty acid-binding protein. Biochemistry 35:7559-7565.
3. 13C NMR study. J Biol Chem 264:2700-2710.
4. Glatz JF, van der Vusse GJ. 1996. Cellular fatty acid-binding proteins: Their function and physiological significance. Prog Lipid Res 35:243-282.
5. 15N-enriched proteins. J Biomol NMR 3:185-204.
6. Herr FM, Aronson J, Storch J. 1996. Role of portal region lysine residues in electrostatic interactions between heart fatty acid binding protein and phospholipid membranes. Biochemistry 35:1296-1303.
7. Hodsdon ME, Cistola DP. 1997a. Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry. Biochemistry 36:1450-1460.
8. 1H exchange. Biochemistry 36:2278-2290.
9. Hodsdon ME, Ponder JW, Cistola DP. 1996. The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: Application of a novel distance geometry algorithm. J Mol Biol 264:585-602.
10. 15N assignments and chemical shift-derived secondary structure of intestinal fatty acid-binding protein. J Biomol NMR 6:198-210.
11. Hsu KT, Storch J. 1996. Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms. J Biol Chem 271:13317-13323.
12. Kim K, Cistola DP, Frieden C. 1996. Intestinal fatty acid-binding protein: The structure and stability of a helix-less variant. Biochemistry 35:7553-7558.
13. Koradi R, Billeter M, Wuthrich K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graph 14:51-55, 29-32.
14. Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8:477-486.
15. Lee B, Richards FM. 1971. The interpretation of protein structures: Estimation of static accessibility. J Mol Biol 55:379-400.
16. Muhandriam DR, Kay LE. 1994. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson B 103:203-216.
17. Sacchettini JC, Gordon JI. 1993. Rat intestinal fatty acid binding protein. A model system for analyzing the forces that can bind fatty acids to proteins. J Biol Chem 268:18399-18402.
18. Sacchettini JC, Gordon JI, Banaszak LJ. 1989. Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli. Proc Natl Acad Sci USA 86:7736-7740.
19. Veerkamp JH, Maatman RG. 1995. Cytoplasmic fatty acid-binding proteins: Their structure and genes. Prog Lipid Res 34:17-52.
20. 13C chemical-shift data. J Biomol NMR 4:171-180.
21. Wishart DS, Sykes BD. 1994b. Chemical shifts as a tool for structure determination. Methods Enzymol 239:363-392.
22. Wishart DS, Sykes BD, Richards FM. 1992. The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651.
23. Wittekind M, Mueller L. 1993. HNCACB, a high sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-and beta-carbon resonances in proteins. J Magn Reson B 101:201-205.