期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2002
卷号：99
期号：19
页码：12055-12060
DOI：10.1073/pnas.192449299
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Corticotropin-releasing factor (CRF), recognized as an important stress factor, binds to a CRF receptor and a CRF-binding protein (CRFBP) that represents a reservoir of endogenous CRF. Although CRFBP was observed to dimerize, at least in part, the ligand was found to be exclusively bound to the monomer--as indicated by photoaffinity labeling. We localized the CRF binding site by using photoaffinity labeling in combination with different mass spectrometric techniques. The amino acid residues Arg-23 and Arg-36 of CRFBP were identified as the sites of photoincorporation of monofunctional and bifunctional photoprobes designed on the basis of the amino acid sequence of human/rat CRF6-33. It was, therefore, concluded that the sequence of amino acid residues 23-36 of CRFBP is involved in ligand binding. Our data are in support of an antiparallel alignment of the photoprobe with the amino acid residues 23-36 of the CRFBP monomer.
