Disulfide bonds Cys9–Cys57, Cys34–Cys88 and Cys38–Cys90 of the β-subunit of human chorionic gonadotropin are crucial for heterodimer formation with the α-subunit: experimental evidence for the conclusions from the crystal structure of hCG
暂无分享,去创建一个
[1] S. Mahale,et al. A detailed study of the L2beta long-loop region of human chorionic gonadotrophin suggests it to be spatially close to, but not part of, the receptor-binding site. , 2002, The Journal of endocrinology.
[2] S. Mahale,et al. Mapping the receptor binding regions of human chorionic gonadotropin (hCG) using disulfide peptides of its beta-subunit: possible involvement of the disulfide bonds Cys(9)-Cys(57) and Cys(23)-Cys(72) in receptor binding of the hormone. , 2001, The journal of peptide research : official journal of the American Peptide Society.
[3] R. Ruddon,et al. Cystine knot mutations affect the folding of the glycoprotein hormone alpha-subunit. Differential secretion and assembly of partially folded intermediates. , 2000, The Journal of biological chemistry.
[4] S. Mahale,et al. Identification of bioneutralization epitopes of human follicle stimulating hormone in the regions 31-52 and 66-75 of its beta-subunit. , 1997, Journal of reproductive immunology.
[5] W. Moyle,et al. The lutropin β-subunit N-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity , 1995, Molecular and Cellular Endocrinology.
[6] D. C. Harris,et al. Crystal structure of human chorionic gonadotropin , 1994, Nature.
[7] W A Hendrickson,et al. Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein. , 1994, Structure.
[8] Usa Serono Symposia,et al. Glycoprotein hormones : structure, function, and clinical implications , 1994 .
[9] P. Roche,et al. A receptor binding site identified in the region 81–95 of the β-subunit of human luteinizing hormone (LH) and chorionic gonadotropin (hCG) , 1993, Molecular and Cellular Endocrinology.
[10] J. R. Huth,et al. Disulfide bond mutations affect the folding of the human chorionic gonadotropin-beta subunit in transfected Chinese hamster ovary cells. , 1993, Journal of Biological Chemistry.
[11] H. Keutmann,et al. A subunit interaction site in human luteinizing hormone: identification by photoaffinity cross-linking. , 1993, Endocrinology.
[12] D. Puett,et al. Replacement of the invariant tyrosine in the CAGY region of the human chorionic gonadotropin β subunit , 1993, Molecular and Cellular Endocrinology.
[13] D. Puett,et al. Mutagenesis of the ‘determinant loop’ region of human choriogonadotropin β , 1993, Molecular and Cellular Endocrinology.
[14] S. Mahale,et al. Search for peptide immunogens of the beta-subunit of human chorionic gonadotropin (hCG) capable of eliciting hormone specific and neutralizing antisera. Identification of an undecapeptide eliciting hCG-specific antisera. , 2009, International journal of peptide and protein research.
[15] J. Dias,et al. Determination of subunit contact-associated epitopes of the beta-subunit of human follicle-stimulating hormone. , 1991, Endocrinology.
[16] K. Miyai,et al. Site-specific mutagenesis of human chorionic gonadotrophin (hCG)-beta subunit: influence of mutation on hCG production. , 1990, Journal of molecular endocrinology.
[17] J. Garnier,et al. Peptide mapping of intersubunit and receptor interactions of human choriogonadotropin , 1990, Molecular and Cellular Endocrinology.
[18] Y. Hayashizaki,et al. Thyroid‐stimulating hormone (TSH) deficiency caused by a single base substitution in the CAGYC region of the beta‐subunit. , 1989, The EMBO journal.
[19] H. Keutmann,et al. Structure-function relationships of gonadotropins. , 1987, Recent progress in hormone research.