ArticleJournal of protein chemistry2003
Modeling and docking of the three-dimensional structure of the human melanocortin 4 receptor.
Article in Journal of protein chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Development of a time-resolved fluorescence probe for evaluation of competitive binding to the cholecystokinin 2 receptor.Bioorganic & medicinal chemistry · 2015Article
- Synthesis and characterization of time-resolved fluorescence probes for evaluation of competitive binding to melanocortin receptors.Bioorganic & medicinal chemistry · 2013Article
- Disturbance of DNA conformation by the binding of testosterone-based platinum drugs via groove-face and intercalative interactions: a molecular dynamics simulation study.BMC structural biology · 2013Article
- A sucrose-derived scaffold for multimerization of bioactive peptides.Bioorganic & medicinal chemistry · 2011Article
- Conformational study on cyclic melanocortin ligands and new insight into their binding mode at the MC4 receptor.European journal of medicinal chemistry · 2011Article
- Interactions of the melanocortin-4 receptor with the peptide agonist NDP-MSH.Journal of molecular biology · 2010Article
- Contribution of the transmembrane domain 6 of melanocortin-4 receptor to peptide [Pro5, DNal (2')8]-gamma-MSH selectivity.Biochemical pharmacology · 2009Article
- Synthesis and evaluation of bivalent NDP-alpha-MSH(7) peptide ligands for binding to the human melanocortin receptor 4 (hMC4R).Bioconjugate chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A three-dimensional structure of the human melanocortin 4 receptor (hMC4R) is constructed in this study using a computer-aided molecular modeling approach. Human melanocortin 4 receptor is a G Protein-Coupled Receptor (GPCR). We structurally aligned transmembrane helices with bovine rhodopsin transmembrane domains, simulated both intracellular and extracellular loop domains on homologous loop regions in other proteins of known 3D structure and modeled the C terminus on the corresponding part of bovine rhodopsin. Then tandem minimization and dynamics calculations were run to refine the crude structure. The simulative model was tested by docking with a triplet peptide (RFF) ligand. It was found that the ligand is located among transmembrane regions TM3, TM4, TM5, and TM6 of hMC4R. In consistence with mutational and biochemical data, binding site is mainly formed as a hydrophobic and negatively charged pocket. The model constructed here might provide a structural framework for making rational predictions in relevant fields.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.