Mutation of any of the four cysteines of D1 (44), Arg 13PRLR , Glu 18PRLR , and Phe 64PRLR (45) were shown to decrease the affinity for PRL by 300-fold or more. It is likely that the loss of binding observed for the cysteine mutants results from structural alterations of D1, because these cysteines are involved in intramolecular disulfide bonds.
by a disulfide bond, was detected. Quanti-tative thiol-disulfide titrations also indicat-ed that oxidized OxyR contains one disul-fide bond (15). We conclude that forma-tion of an intramolecular (16) disulfide bond between residues Cys199 and Cys208 leads to the conformational change that activates the OxyR transcription factor. Chon Hwa TSAI-MORRIS Ph.D. National Institutes of Intramolecular Disulfide Bonds of the Prolactin Receptor Short Form Are Required for Its Inhibitory Action on the Function of the Long Form of the Receptor Article Full-text available
The CD132 Cys183Cys232 disulfide bond is cleaved on the surface of cultured T cells by protein reductants and on the surface of thymocytes in mice after an inflammatory challenge. 46 The disulfide bond is located at the subunit surface close to the IL-2 binding site. 47 Reduction of the disulfide 46 or replacement of Cys183 and Cys232 with Development and Potential Clinical Uses of Human Prolactin May 01, 2005 · In humans, the PRL gene is located on chromosome 6 and encodes a mature protein of 199 amino acids (23 kDa), including six cysteine residues involved in three intramolecular disulfide bonds. PRL shares high structural and functional similarity with two other polypeptide hormones, GH and placental lactogen (PL).
Dec 01, 2015 · The most prominent structural characteristic of GH/PRL family is the conserved intramolecular disulfide bonds. All reported SLs, PRL2s (except for cmPRL2) and tetrapod PRL1s contain three disulfide bonds, while GHs and teleost PRL1s have only two disulfide bonds, lacking one in the N-terminus and a subsequent small loop structure (see Manzon Impact of subdomain D1 of the short form S1b of the human Jul 01, 2014 · The prolactin receptor (PRLR) as stabilized by two intramolecular disulfide bonds located in the interior of the D1 subdomain, is required for its inhibitory action on Prl-induced LF-mediated signal transduction function . However,
Long dynamics simulations were carried out on the B1 immunoglobulinbinding domain of streptococcal protein G (ProtG) and bovine pancreatic trypsin inhibitor (BPTI) using atomistic descriptions of th Mechanisms of Transient Signaling via Short and Long Nov 29, 2013 · It has previously been shown that two intramolecular disulfide (S-S) bonds within the extracellular subdomain 1 (D1; see Fig. 8 A) of PRLR-S contributes to the inhibition of PRLR-L functions . Our data imply that intracellular domain(s) of PRLR-L located within the 293430 amino acid region are involved in inhibition of PRLR-S transient effects ( Fig. 8 D ).
Nov 29, 2013 · Xie Y. L., Hassan S. A., Qazi A. M., Tsai-Morris C. H., Dufau M. L. (2009) Intramolecular disulfide bonds of the prolactin receptor short form are required for its inhibitory action on the function of the long form of the receptor. Mol. Cell. Biol. 29, 25462555 [PMC free article] OPEN ACCESS JOURNAL AT INIST-CNRS Gene SectionIntramolecular disulfide bonds of the prolactin receptor short form are required for its inhibitory action on the function of the long form of the receptor. Mol Cell Biol. 2009 May;29(10):2546-55 Goffin V, Bogorad RL, Touraine P. Identification of gain-of-function variants of the human prolactin receptor. Methods
The six cystein residues in PRL undergo oxidation and form stable, successive intramolecular disulfide bonds. Besides, a proportion of pituitary and circulating PRL is glycosylated in most species. Approximately 20% of circulating human PRL is glycosylated through N-linkage at position 31 (Lewis et al. 1985; Champier, Claustrat, Sassolas, and Prolactin:Structure, Function, and Regulation of The prolactin molecule is arranged in a single chain of amino acids with three intramolecular disulfide bonds between six cysteine residues (Cys 4-Cys 11, Cys 58-Cys 174, and Cys 191-Cys 199 in humans) . The sequence homology can vary from the striking 97% among primates to as low as 56% between primates and rodents .
Intramolecular disulfide bonds of the prolactin receptor short form are required for its inhibitory action on the function of the long form of the receptor. Mol Cell Biol. 2009;29:2546-2555. Sheng Y, Tsai Morris C-H, Li J, Dufau ML. Structure of SARS-CoV-2 ORF8, a rapidly evolving immune Jan 12, 2021 · The structure of the SARS-CoV-2 ORF8 protein reveals two novel intermolecular interfaces layered onto an ORF7 fold. One is mediated by a disulfide bond, the other is noncovalent, and both are novel with respect to SARS-CoV. The structural analysis here establishes a molecular framework for understanding the rapid evolution of ORF8, its
The dimerization of single-chain receptors has been shown to be noncovalent such as with the GHR 17 but also covalent involving disulfide bonds as with the EPOR.74 With the IL-6R and CNTFR the heterodimerization of the ligand binding, nonsignaling subunits to gp130 is noncovalent; however, the association between the signaling subunits (PDF) Intramolecular Disulfide Bonds of the Prolactin Intramolecular Disulfide Bonds of the Prolactin Receptor Short Form Are Required for Its Inhibitory Action on the Function of the Long Form of the Receptor