Functional relationship of serine 90 phosphorylation and the surrounding putative salt bridge in bovine prolactin

Molecular and Cellular Endocrinology

Volumn 204, Issue 1-2, 2003, Pages 117-125

  Schenck, E J H ^a   Canfield, J M ^a   Brooks, C L ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

Bovine; Phosphorylation; Prolactin; Salt bridge

Indexed keywords

GLUTAMIC ACID; PROLACTIN; SERINE; SERINE 90; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; BINDING AFFINITY; CELL ASSAY; CELL LINE; EXPERIMENT; FUNCTIONAL ASSESSMENT; HYDROPHOBICITY; IN VIVO STUDY; MUTATION; NONHUMAN; PHOSPHORYLATION; POLARIZATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN LOCALIZATION; RECEPTOR BINDING; SUBSTITUTION REACTION;

EID: 0038783615     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(03)00123-0     Document Type: Article

References (31)

1. Aramburo C., Montiel J.L., Proudman J.A., Scanes C.G. Phosphorylation of prolactin and growth hormone. J. Mol. Endocrinol. 8:1992;183-191.
2. Bazan J.F. Structural design of molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA. 87:1990;6934-6938.
3. Brooks C.L., Saiduddin S. Phosphorylation of bovine prolactin eliminates luteotropic activity in the rat. Life Sci. 63:1998;1281-1287.
4. Brooks C.L., Isaacs L.A., Wicks J.R. Preparative purification of phosphorylated and nonphosphorylated bovine prolactin. Mol. Cell. Endocrinol. 99:1994;301-305.
5. Chakrabartty A., Baldwin R.L. Stability of α-helices. Adv. Prot. Chem. 46:1995;141-176.
6. Chantalat L., Jones N.D., Korber F., Navaza J., Pavlovsky A.G. The crystal-structure of wild-type growth hormone at 2.5 angstrom resolution. Prot. Peptide Let. 2:1995;333-349.
7. Clackson T., Ultsch M.H., Wells J.A., de Vos A.M. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. 277:1998;1111-1128.
8. Creighton T.E. Proteins: Structure and Molecular Properties. Second edition: 1993;W.H. Freeman and Company, New York.
9. de Vos A.M., Ultsch M., Kossiakoff A.A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 255:1992;306-312.
10. Duda K.M., Brooks C.L. Human growth hormone site 2 lactogenic activity requires a distant tyrosine 164. FEBS Lett. 449:1999;120-124.
11. Gertler A., Grosclaude J., Strasburger C.J., Nir S., Djiane J. Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization. J. Biol. Chem. 271:1996;24482-24491.
12. Goffin V., Kelly P.A. The prolactin/growth hormone receptor family: structure/function relationships. J. Mammary Gland Biol. Neopl. 2:1997;7-17.
13. Goffin V., Struman I., Mainfroid V., Kinet S., Martial J.A. Evidence for a second receptor binding site on human prolactin. J. Biol. Chem. 269:1994;32598-32606.
14. Goffin V., Kinet S., Ferrag F., Binart N., Martial J.A., Kelly P.A. Antagonistic properties of human prolactin analogues that show paradoxical agonist activity in the NB-2 cell. J. Biol. Chem. 271:1996;16573-16579.
15. Ilondo M.M., Damholt A.B., Cunningham B.C., Wells J.A., De Meyts P., Shymko R.M. Receptor dimerization determines the effects of growth hormone in primary rat adipocytes and cultured human IM-9 lymphocytes. Endocrinology. 134:1994;2397-2403.
16. Halaby D., Thoreau E., Djiane J., Mornon J.-P. Homology modeling of rabbit prolactin hormone complexed with its receptor. Proteins. 27:1997;459-468.
17. Kim B.G., Brooks C.L. Isolation and characterization of phosphorylated bovine prolactin. Biochem. J. 296:1993;41-47.
18. Kunkel T.A., Bebenek K., McClary J. Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204:1991;125-139.
19. .Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
20. Luck D.N., Gout P.W., Kelsay K., Atkinson T., Beer C.T., Smith M. Recombinant methionyl bovine prolactin: loss of bioactivity after single amino acid deletions from putative helical regions. Mol. Endocrinol. 4:1990;1011-1016.
21. Maciejewski P.M., Peterson F.C., Anderson P.J., Brooks C.L. Mutation of serine 90 to glutamic acid mimics phosphorylation of bovine prolactin. J. Biol. Chem. 270:1995;27661-27665.
22. Munson P.J., Rodbard D. LIGAND: A versatile computerized approach for characterization of ligand binding systems. Anal. Biochem. 107:1980;220-239.
23. Peterson F.C., Anderson P.J., Berliner L.J., Brooks C.L. Expression, folding, and characterization of small proteins with increasing disulfide complexity by a pT7-7-derived phagemid. Prot. Express. Purif. 15:1999;16-23.
24. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA. 74:1977;5463-5467.
25. Sinha Y.N. Structural variants of prolactin: occurrence and physiological significance. Endo. Rev. 16:1995;354-369.
26. Smith P.K., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., Klenk D.C. Measurement of protein using bicinchroninic acid. Anal. Biochem. 150:1985;76-85.
27. Somers W., Ultsch M., de Vos A.M., Kossiakoff A.A. The X-ray structure of a growth hormone-prolactin receptor complex. Nature. 372:1994;478-481.
28. Sundstrom M., Lundqvist T., Rodin J., Giebel L.B., Milligan D., Norstedt G. Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 Å resolution. J. Biol. Chem. 271:1996;32197-32203.
29. Tanaka T., Shiu R.P.C., Gout P.W., Beer C.T., Noble T.L., Friesen H.G. A new sensitive and specific bioassay for lactogenic hormones: measurement of prolactin and growth hormone in human serum. J. Clin. Endocrinol. Metab. 51:1980;1058-1063.
30. Walker A.M. Phosphorylated and nonphosphorylated prolactin isoforms. Trends Endocrinol Metab. 5:1994;195-200.
31. Wicks J.R., Brooks C.L. Biological activity of phosphorylated and dephosphorylated bovine prolactin. Mol. Cell. Endocrinol. 112:1995;223-232.