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PRODID:-//Virginia Tech//VT Calendar//EN
BEGIN:VEVENT
DTSTAMP:20120912T202000Z
UID:1345560539668@events.msu.edu
CATEGORIES:Conferences / Seminars / Lectures
DTSTART:20120912T202000Z
DTEND:20120913T035900Z
SUMMARY:MAX T. ROGERS DISTINGUISHED LECTURESHIP IN CHEMISTRY
DESCRIPTION:
 The MAX T. ROGERS DISTINGUISHED LECTURESHIP welcomes 
 a lecture by Professor Raymond Charles 
 Stevens, Departments of Molecular Biology and 
 Chemistry, The Scripps Research Institute, 
 La Jolla, CA\n
 \n
 Molecular Recognition and Signaling 
 in the Human GPCR Superfamily\n
 \n
 Abstract\n
 \n
 GPCRs 
 constitute one of the largest protein 
 families in the human genome and play essential 
 roles in normal cell processes, most 
 notably in cell signaling. The human GPCR family 
 contains more than 800 members and recognizes 
 thousands of different ligands and activates 
 a number of signaling pathways through 
 interactions with a small number of binding partners. 
 GPCRs have also been implicated in numerous 
 human diseases, and represent more than 
 30-40% of drug targets. Delivering GPCR structures 
 in close collaboration with the community 
 on specific receptor systems is of immense 
 value to the basic science community interested 
 in cell signaling and molecular recognition, 
 as well as the applied science community 
 interested in drug discovery. This work is 
 being followed up with additional biophysical 
 characterization including NMR spectroscopy 
 and community wide assessments with computational 
 biology groups throughout the world.  Crystal 
 structures are now available for rhodopsin, 
 adrenergic, and adenosine receptors in 
 both inactive and activated forms, as well as 
 for chemokine, dopamine, histamine, S1P1 and 
 opioid receptors in inactive conformations. 
 A review of the common structural features seen 
 in these receptors and the scope of structural 
 diversity of GPCRs at different levels of 
 homology provides insight into our growing 
 understanding of the biology of GPCR action and 
 their impact on drug discovery.  Given the 
 current set of GPCR structural data, a distinct 
 modularity is now being observed between 
 the extracellular (ligand-binding) and intracellular 
 (signaling) regions. The rapidly expanding 
 repertoire of GPCR structures provides 
 a solid framework for experimental and molecular 
 modeling studies, and helps to chart a roadmap 
 for comprehensive structural coverage of 
 the whole superfamily and an understanding 
 of GPCR biological and therapeutic mechanisms. 
  \n
 \n
 This work was supported by NIGMS PSI:Biology 
 for GPCR structure processing (U54GM094618) 
 and the NIH Roadmap Initiative (JCIMPT) 
 for technology development (GM073197). \n\n
 Price: free\n
 Sponsor: Chemistry\n
 Sponsor's Homepage: http://www.chemistry.msu.edu/\n
 Contact name: Rebecca Townsend\n
 Contact phone: 517.355.9175 x345\n
 Contact email: townsend@chemistry.msu.edu\n
LOCATION:138 Chemistry Building
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