Probing the retinol-binding site of bovine beta-lactoglobulin.
作者： Y. Cho , C.A. Batt , L. Sawyer
DOI: 10.1016/S0021-9258(19)78097-1
关键词:
摘要: The retinol-binding site of beta-lactoglobulin has been located by selective modification amino acid residues which reside in the two putative binding sites. Based upon separate crystallographic analyses bovine beta-lactoglobulin, different sites for retinol have proposed: one proposal favors an interior cavity, other a surface cleft. To discriminate between these models, we made four site-directed mutations introducing W19A or K70M pocket and F136A K141M pocket. exhibited marked decrease its retinoic compared to F136A, K141M, wild-type proteins. Retinyldenepropylamine, retinyl Schiff base analog retinol, was synthesized absorption spectrum when bound wild-type, K70M, proteins examined probe interaction with respective lysine residues. retinylidenepropylamine kinetic red shift as distinct from blue observed it is either beta-lactoglobulins. indicates protonation base. resulting tagged peptide isolated after cyanogen bromide cleavage found be Ala25-Met107 peptide, consistent Lys70 being residue interacts retinol. These results support that binds evolutionarily conserved cavity rather than
sci-hub.st 参考文章(29)
D.M. White, D.D. Mikol, R Espinosa, B Weimer, M.M. Le Beau, K Stefansson, Structure and chromosomal localization of the human gene for a brain form of prostaglandin D2 synthase. Journal of Biological Chemistry. ,vol. 267, pp. 23202- 23208 ,(1992) , 10.1016/S0021-9258(18)50077-6
B Redl, P Holzfeind, F Lottspeich, cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily. Journal of Biological Chemistry. ,vol. 267, pp. 20282- 20287 ,(1992) , 10.1016/S0021-9258(19)88698-2
Simak Ali, A John Clark, None, Characterization of the gene encoding ovine beta-lactoglobulin: similarity to the genes for retinol binding protein and other secretory proteins Journal of Molecular Biology. ,vol. 199, pp. 415- 426 ,(1988) , 10.1016/0022-2836(88)90614-6
Sidney Futterman, Joram Heller, The Enhancement of Fluorescence and the Decreased Susceptibility to Enzymatic Oxidation of Retinol Complexed with Bovine Serum Albumin, β-Lactoglobulin, and the Retinol-binding Protein of Human Plasma Journal of Biological Chemistry. ,vol. 247, pp. 5168- 5172 ,(1972) , 10.1016/S0021-9258(19)44953-3
M Hirose, T Akuta, N Takahashi, Renaturation of ovotransferrin under two-step conditions allowing primary folding of the fully reduced form and the subsequent regeneration of the intramolecular disulfides. Journal of Biological Chemistry. ,vol. 264, pp. 16867- 16872 ,(1989) , 10.1016/S0021-9258(19)84787-7
Eric Dufour, Michael C. Marden, Tomasz Haertlé, β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites FEBS Letters. ,vol. 277, pp. 223- 226 ,(1990) , 10.1016/0014-5793(90)80850-I
S Pervaiz, K Brew, Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science. ,vol. 228, pp. 335- 337 ,(1985) , 10.1126/SCIENCE.2580349
W. GU, J.W. Brady, Molecular dynamics simulations of the whey protein ß-lactoglobulin Protein Engineering. ,vol. 5, pp. 17- 27 ,(1992) , 10.1093/PROTEIN/5.1.17
Robert Huber, Monika Schneider, Otto Epp, Irmgard Mayr, Albrecht Messerschmidt, James Pflugrath, Hartmut Kayser, Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. Journal of Molecular Biology. ,vol. 195, pp. 423- 434 ,(1987) , 10.1016/0022-2836(87)90661-9
Robert Jenness, Comparative aspects of milk proteins. Journal of Dairy Research. ,vol. 46, pp. 197- 210 ,(1979) , 10.1017/S0022029900017040