2010 Ligand Recognition and Molecular Gating Gordon Research Conference
2010 Ligand Recognition and Molecular Gating Gordon Research Conference
批准号:
7902671
负责人:
Nancy Ryan Gray
金额:
$2.0万
依托单位国家:
美国
项目类别:
财政年份:
2010
资助国家:
美国
项目状态:
已结题
起止时间:
2010-04-01 至 2010-05-21
关键词:
ATP-Binding Cassette TransportersAddressAreaBindingCardiovascular DiseasesCommunitiesConnexinsDataDevelopmentG-Protein-Coupled ReceptorsGTP-Binding ProteinsGated Ion ChannelGoalsHealthIntegral Membrane ProteinInternationalIon ChannelIonsItalyKnowledgeLigand BindingLigandsLipidsMalignant NeoplasmsMembraneMembrane ProteinsMembrane Structure and FunctionMental DepressionMethodsMolecular ConformationNeurodegenerative DisordersPharmacologic SubstanceProtein BindingProteinsReceptor ActivationResearchResearch PersonnelResolutionScienceSeriesSignal TransductionStructureVisionchemotherapeutic agentdeafnessdesignintercellular communicationmolecular recognitionnervous system disordernovel therapeuticsprogramsprotein structureprotein structure functionpublic health relevanceresearch studyskin disordersmall moleculesymposiumvoltage
中文摘要
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英文摘要
DESCRIPTION (provided by applicant): The Gordon Research Conference on Ligand Recognition and Molecular Gating will be held on May 16 - 21, 2010 in Il Ciocco, Italy. The broad and long term goal of the conference is to increase our understanding of how integral membrane proteins bind ligands (ions, small molecules, proteins) and transmit signals across membranes. The conference main objective is to share the newest knowledge on ion channels, G- protein coupled receptors, and transporters of all types, with emphasis on combining high resolution structural data with functional and theoretical data to probe gating or activation by ligands of these proteins. A unifying theme in these three different classes of membrane proteins is that ligand binding, gating, and/or transport involves conformational changes. The characterization of defined, mechanistically relevant conformations of fully functional protein will be a focus of the 2010 conference. The program will have 40 speakers, well-established leaders in the field of membrane protein research as well as promising young investigators. A keynote presentation and eight sessions will broadly address structure and mechanism of secondary transporters, ligand-gated and voltage-gated ion channels, channels of intercellular communication, passages through the outer membrane, membrane-protein lipid interactions, new methods probing membrane protein structures and conformations, and G-protein coupled receptor activation and interaction with G proteins and ligands. The Gordon Research Conference on Ligand Recognition and Molecular Gating is a critical component of the series of conferences that drive research in the international community of membrane protein structure/function researchers. The health relatedness of this application is that well over 50% of current pharmaceutical targets are integral membrane proteins of the types discussed at this conference, with structural and functional descriptions directly relevant to the design of new chemotherapeutic agents. The impact areas range from cancer (ABC transporters), vision/ depression/cardiovascular diseases (G-protein coupled receptors), neurodegenerative diseases, skin diseases, deafness, and developmental abnormalities (connexins) to neurological diseases (ion channels).
PUBLIC HEALTH RELEVANCE: The health relatedness of this application is that well over 50% of current pharmaceutical targets are integral membrane proteins of the types discussed at this conference. Understanding the structure and function of these membrane bound molecules is one of the most important goals of the 21st century, both for science and for development of new therapeutics. Results discussed and new experiments designed have impact on areas such as cancer (ABC transporters), vision/ depression/ cardiovascular diseases (G-protein coupled receptors), neurodegenerative diseases, skin diseases, deafness, and developmental abnormalities (connexins) to neurological diseases (ion channels).
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