Title : Steroid-induced conformational changes of rat glucocorticoid receptor cause altered trypsin cleavage of the putative helix 6 in the ligand binding domain.

Pub. Date : 1999 Sep 10

PMID : 10580842






4 Functional Relationships(s)
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1 Steroid-induced conformational changes of rat glucocorticoid receptor cause altered trypsin cleavage of the putative helix 6 in the ligand binding domain. Steroids nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
2 This was supported by the observation that trypsin digestion of the steroid-free R651A mutant GR gave rise to the 30-kDa meroreceptor (amino acids 518-795), which displayed wild type affinity. Steroids nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
3 This 30-kDa species is thus the smallest non-associated fragment of GR possessing wild type steroid binding affinity. Steroids nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus
4 However, unlike the estrogen receptor or the more closely related progesterone receptor, the precise proteolytic cleavage points of both the steroid-free and -bound GR fall within regions that are predicted, on the basis of X-ray crystal structures of related receptors, to be alpha-helical and resistant to proteolysis. Steroids nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus