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Title:
Pharmacophore model for bile acids recognition by the FPR receptor | Journal of Computer-Aided Molecular Design
Description:
Formyl-peptide receptors (FPRs) belong to the family A of the G-protein coupled receptor superfamily and include three subtypes: FPR, FPR-like-1 and FPR-like-2. They have been involved in the control of␣many inflammatory processes promoting the recruitment and infiltration of leukocytes in regions of inflammation through the molecular recognition of chemotactic factors. A large number of structurally diverse chemotypes modulate the activity of FPRs. Newly identified antagonists include bile acids deoxycholic acid (DCA) and chenodeoxycholic acid (CDCA). The molecular recognition of these compounds at FPR receptor was computationally investigated using both ligand- and structure-based approaches. Our findings suggest that all antagonists bind at the first third of the seven helical bundles. A closer inspection of bile acid interaction reveals a number of unexploited anchor points in the binding site that may be used to aid the design of new potent and selective bile acids derivatives at FPR.
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Keywords {🔍}
article, google, scholar, cas, bile, receptor, acids, receptors, chem, molecular, wang, recognition, fpr, acid, access, pharmacol, privacy, cookies, content, journal, macchiarulo, costantino, pellicciari, immunol, med, mol, publish, search, design, exp, murphy, oppenheim, data, information, log, research, pharmacophore, ferrari, roberto, formylpeptide, antagonists, selective, open, discover, biol, res, gong, shen, chen, biochem,
Topics {✒️}
bile acids recognition formyl peptide receptor month download article/chapter gabriele costantino & roberto pellicciari molecular recognition molecular operating environment pharmacophore model bile acids nlrp3 inflammasome pathway antagonists bind related subjects fxr selective modulation full article pdf privacy choices/manage cookies check access instant access european economic area inflammatory processes promoting structure-based approaches unexploited anchor points van der velde fatty acids conditions privacy policy design tecnologia del farmaco università di perugia article ferrari accepting optional cookies miettinen hm roberto pellicciari chenodeoxycholic acid article journal journal finder publish main content log pharmacology mills js article log author correspondence fpr receptor article cite mangelsdorf dj privacy policy personal data books a optional cookies manage preferences wang jm journal publish mol cell 5 mol cell 3
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headline:Pharmacophore model for bile acids recognition by the FPR receptor
description:Formyl-peptide receptors (FPRs) belong to the family A of the G-protein coupled receptor superfamily and include three subtypes: FPR, FPR-like-1 and FPR-like-2. They have been involved in the control of␣many inflammatory processes promoting the recruitment and infiltration of leukocytes in regions of inflammation through the molecular recognition of chemotactic factors. A large number of structurally diverse chemotypes modulate the activity of FPRs. Newly identified antagonists include bile acids deoxycholic acid (DCA) and chenodeoxycholic acid (CDCA). The molecular recognition of these compounds at FPR receptor was computationally investigated using both ligand- and structure-based approaches. Our findings suggest that all antagonists bind at the first third of the seven helical bundles. A closer inspection of bile acid interaction reveals a number of unexploited anchor points in the binding site that may be used to aid the design of new potent and selective bile acids derivatives at FPR.
datePublished:2006-09-14T00:00:00Z
dateModified:2006-09-14T00:00:00Z
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Antagonists
Bile acids
Formyl-peptide receptors
G-protein coupled receptors
Molecular modeling
Molecular recognition
Pharmacophore
Rational drug design
Physical Chemistry
Computer Applications in Chemistry
Animal Anatomy / Morphology / Histology
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headline:Pharmacophore model for bile acids recognition by the FPR receptor
description:Formyl-peptide receptors (FPRs) belong to the family A of the G-protein coupled receptor superfamily and include three subtypes: FPR, FPR-like-1 and FPR-like-2. They have been involved in the control of␣many inflammatory processes promoting the recruitment and infiltration of leukocytes in regions of inflammation through the molecular recognition of chemotactic factors. A large number of structurally diverse chemotypes modulate the activity of FPRs. Newly identified antagonists include bile acids deoxycholic acid (DCA) and chenodeoxycholic acid (CDCA). The molecular recognition of these compounds at FPR receptor was computationally investigated using both ligand- and structure-based approaches. Our findings suggest that all antagonists bind at the first third of the seven helical bundles. A closer inspection of bile acid interaction reveals a number of unexploited anchor points in the binding site that may be used to aid the design of new potent and selective bile acids derivatives at FPR.
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Bile acids
Formyl-peptide receptors
G-protein coupled receptors
Molecular modeling
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Rational drug design
Physical Chemistry
Computer Applications in Chemistry
Animal Anatomy / Morphology / Histology
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