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• W2000475852 abstract "Efforts to identify the manner in which human choriogonadotropin (hCG) contacts lutropin receptors (LHR) have been stymied by the complex structure of the hormone and the likelihood that it contacts the receptor at multiple sites. During studies of hCG assembly in mammalian cells, we found that addition of a cysteine to the long disordered β-subunit COOH terminus (βCT) enabled it to become cross-linked by a disulfide to cysteines that are substituted for residues in loop α2 or in the α-subunit COOH terminus (αCT). This created a knob on the α-subunit at the location of the cysteine. Knobs of various sizes and charges were useful for probing surfaces of the α-subunit thought previously to contact the LHR. Attachment of the βCT to residues in loop α2 facing loops β1 and β3 reduced hormone activity only a few fold revealing that this surface does not participate in essential high affinity receptor contacts, a finding inconsistent with our earlier view of the hCG-LHR complex. In contrast, this approach showed that the opposite surface of loop α2 appeared to be nearer the receptor interface. Although attachment of knobs to portions of the αCT reduced hormone activity substantially, this finding was difficult to interpret. As discussed, this procedure should be adapted readily to other proteins and may facilitate the introduction of fluorophores, enzymes, or other reagents at specific sites on protein surfaces. It may also permit one to cross-link proteins or to obscure specific protein surfaces during the development of Trojan Horse therapeutics." @default.
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• W2000475852 date "2004-10-01" @default.
• W2000475852 modified "2023-09-28" @default.
• W2000475852 title "Use of Protein Knobs to Characterize the Position of Conserved α-Subunit Regions in Lutropin Receptor Complexes" @default.
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• W2000475852 doi "https://doi.org/10.1074/jbc.m406931200" @default.
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