Molecular Modeling of Transmembrane Helices 6 and 7 of the Heptahelical Lutropin Receptor
| Autor: | David Puett, J P Simon, Krassimira Angelova |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Conformational change DNA Complementary Molecular model Protein Conformation Stereochemistry Mutant Plasma protein binding Biochemistry Protein structure Structural Biology Cyclic AMP Animals Receptor Chemistry Cell Membrane Water Hydrogen Bonding General Medicine Receptors LH Protein Structure Tertiary Rats Transmembrane domain COS Cells Mutation Mutagenesis Site-Directed Protons Signal transduction Protein Binding Signal Transduction |
| Zdroj: | Protein & Peptide Letters. 9:153-158 |
| ISSN: | 0929-8665 |
| Popis: | In response to ligand binding and activating mutations, the lutropin receptor undergoes a conformational change to trigger a cellular response. D556 is the most common locus for naturally occurring activating mutations of the lutropin receptor, and a D556A mutant is shown to be constitutively active. A water-mediated proton transfer is postulated as part of the transmembrane signaling mechanism. Using energy minimization and ab initio calculations, a hydrogen bonding network involving a highly constrained water molecule(s) and D556 (helix 6) and N593 / N597 / Y601 (helix 7) is presented. |
| Databáze: | OpenAIRE |
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