Pictured: Stephen B. Long, PhD
Office phone:
212-639-2903
Laboratory phone:
212-639-2959
E-mail:
longs@mskcc.org
Research topics:
Cancer Therapeutics & Drug Development; Cell Signaling; Chemistry, Biochemistry & Chemical Biology; Genetics & Genomics; Protein Folding & Trafficking; Structural Biology

Our laboratory is a basic research laboratory that uses a combination of x-ray crystallography, biochemistry, and electrophysiology to study eukaryotic membrane proteins.  Our objective is to understand the molecular mechanisms of ion channels and membrane-embedded enzymes that have crucial biological functions and have been implicated in diseases including cardiac arrhythmia, immune disorders, and cancer.  The focus on eukaryotic membrane proteins that do not have prokaryotic counterparts is further motivated because unique aspects of biology surround them and because their 3D structures and molecular mechanisms represent uncharted territory.  For ion channels, we seek to address fundamental issues relating to the ways in which potassium, calcium, and chloride channels conduct ions across cellular membranes, how the channels achieve ion selectivity, and the mechanisms for how they are gated by ligands, properties of the membrane, and protein-protein interactions.  For membrane-embedded enzymes, which catalyze chemical reactions within the environment of lipid membranes, the salient questions include how both water-soluble and lipophilic substrates access the catalytic active site, what conformational changes in the enzyme occur, and what constraints the lipid membrane places on these.  

If you are interested in joining the laboratory, please e-mail Stephen Long.  There are openings for postdoctoral fellows and those with excellent credentials in x-ray crystallography or electrophysiology are especially encouraged to apply.  Prospective graduate students are encouraged to apply to the Gerstner Sloan-Kettering Graduate School of Biomedical Sciences and/or the Weill Cornell Graduate School of Medical Sciences.

structure of the calcium release-activated calcium (CRAC) channel Orai and the structure of the two-pore domain potassium channel K2P1 (TWIK-1)