Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1,8-anilinonaphthalene-8-sulfonate

Biophysical Journal

Volumn 77, Issue 2, 1999, Pages 1107-1116

  Ory, Jeramia J ^a,b   Banaszak, Leonard J ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; FATTY ACID; FLUORESCENT DYE; LIPID BINDING PROTEIN; WATER;

ADIPOCYTE; ANIMAL CELL; ARTICLE; BINDING SITE; CALORIMETRY; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; ENTHALPY; FLUORESCENCE; KINETICS; LIGAND BINDING; MOUSE; NONHUMAN; PROTEIN CONFORMATION; THERMODYNAMICS;

ANIMALIA;

EID: 0032774245     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76961-4     Document Type: Article

References (28)

1. Banaszak, L., N. Winter, Z. Xu, D. A. Bernlohr, S. Cowan, and T. A. Jones. 1994. Lipid-binding proteins: a family of fatty acid and retinoid transport proteins. Adv. Protein Chem. 45:89-151.
2. Brunger, A. T. 1988. Crystallographic refinement by simulated annealing. Application to a 2.8 Å resolution structure of aspartate aminotransferase. J. Mol. Biol. 203:803-816.
3. Brunger, A. T. 1992. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:472-474.
4. Brunger, A. T., J. Kuriyan, and M. Karplus. 1987. Crystallographic R factor refinement by molecular dynamics. Science. 235:458-460.
5. Carter, C. W. J., and C. W. Carter. 1979. Crystallization using incomplete factorial experiments. J. Biol. Chem. 254:12219-12223.
6. Cistola, D. P., K. Kim, H. Rogl, and C. Frieden. 1996. Fatty acid interactions with a helix-less variant of intestinal fatty acid-binding protein. Biochemistry. 35:7559-7565.
7. Constantine, K. L., M. S. Friedrichs, M. Wittekind, H. Jamil, C. H. Chu, R. A. Parker, V. Goldfarb, L. Mueller, and B. T. Farmer II. 1998. Backbone and side chain dynamics of uncomplexed human adipocyte and muscle fatty acid-binding proteins. Biochemistry. 37:7965-7980.
8. Dang, Q., and C. Frieden. 1997. New PC versions of the kinetic-simulation and fitting programs, KINSIM and FITSIM. Trends Biochem. Sci. 22: 317.
9. Hodsdon, M. E., and D. P. Cistola. 1997. 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.
10. Jancarik, J., and S. H. Kim. 1991. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411.
11. Jiang, J. S., and A. T. Brunger. 1994. Protein hydration observed by x-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243:100-115.
12. Johnson, J. D., M. A. El-Bayoumi, L. D. Weber, and A. Tulinsky. 1979. Interaction of alpha-chymotrypsin with the fluorescent probe 1- anilinonaphthalene-8-sulfonate in solution. Biochemistry. 18:1292-1296.
13. Kane, C. D., and D. A. Bernlohr. 1996. A simple assay for intracellular lipid-binding proteins using displacement of 1-anilinonaphthalene 8-sulfonic acid. Anal. Biochem. 233:197-204.
14. Kirk, W. R., E. Kurian, and F. G. Prendergast. 1996. Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1′)anilinonaphthalene binding to intestinal fatty acid binding protein. Biophys. J. 70: 69-83.
15. Kleywegt, G. J., and T. A. Jones. 1994. VOIDOO reference. Acts. Crystallogr. D. 50:178-185.
16. Koradi, R., M. Billeter, and K. Wuthrich. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics. 14:51-55, 29-32.
17. Kurian, E., W. R. Kirk, and F. G. Prendergast. 1996. Affinity of fatty acid for rat intestinal fatty acid binding protein: further examination. Biochemistry. 35:3865-3874.
18. LaLonde, J. M., D. A. Bernlohr, and L. J. Banaszak. 1994a. X-ray crystallographic structures of adipocyte lipid-binding protein complexed with palmitate and hexadecanesulfonic acid. Properties of cavity binding sites. Biochemistry. 33:4885-4895.
19. LaLonde, J. M., M. A. Levenson, J. J. Roe, D. A. Bernlohr, and L. J. Banaszak. 1994b. Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and x-ray crystallographic studies. J. Biol. Chem. 269:25339-25347.
20. Liang, J., H. Edelsbrunner, and C. Woodward. 1998. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Sci. 7:1884-1897.
21. LiCata, V., and D. Bernlohr. 1998. Surface properties of adipocyte lipid-binding protein: response to lipid binding and comparison with homologous proteins. Proteins. 33:577-589.
22. McDonald, I. K., and J. M. Thornton. 1994. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238.
23. Ory, J., C. D. Kane, M. A. Simpson, L. J. Banaszak, and D. A. Bernlohr. 1997. Biochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding protein. J. Biol. Chem. 272:9793-9801.
24. Ory, J. J., A. Mazhary, H. Kuang, R. R. Davies, M. D. Distefano, and L. J. Banaszak. 1998. Structural characterization of two synthetic catalysts based on adipocyte lipid binding protein. Protein Eng. 11:253-261.
25. Slavik, J., J. Horak, L. Rihova, and A. Kotyk. 1982. Anilinonaphthalene sulfonate fluorescence and amino acid transport in yeast. J. Membr. Biol. 64:175-179.
26. Tonomura, B., H. Nakatani, M. Ohnishi, J. Yamaguchi-Ito, and K. Hiromi. 1978. Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid. Anal. Biochem. 84:370-383.
27. Weber, L., A. Tulinsky, J. Johnson, and M. El-Bayoumi, 1979. Expression of functionality of alpha-chymotrypsin. The structure of a fluorescent probe-alpha-chymotrypsin complex and the nature of its pH dependence. Biochemistry. 18:1297-1303.
28. Xu, Z. H., M. K. Buelt, L. J. Banaszak, and D. A. Bernlohr. 1991. Expression, purification, and crystallization of the adipocyte lipid binding protein. J. Biol. Chem. 266:14367-14370.