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NINDSNIMHNICHDNIDCDNEINIDCRNIANIAAANIDANHGRI NCCIHNIDDKNIEHSCCB

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Investigator

Anirban Banerjee, Ph.D.

Unit on Structural & Chemical Biology of Membrane Proteins


Building 35-A Room 2F-127
35A Convent Drive
Bethesda MD 20892
Office: 301-496-4855


anirban.banerjee@nih.gov

Dr. Anirban Banerjee received his B.Sc. (Honours) from Jadavpur University, India and his M.Sc. in Chemistry from the Indian Institute of Technology, Kanpur. This early training culminated in a Ph.D. in Chemical Biology in Greg Verdine's lab in the Chemistry and Chemical Biology Department at Harvard University. In his graduate thesis work, Dr. Banerjee worked on the mechanism of damaged base recognition and catalysis by DNA glycosylases, enzymes that initiate the process of base excision repair of DNA. In his post doctoral research in Rod MacKinnon's laboratory at The Rockefeller University, Dr. Banerjee focused on several aspects of the mechanism of voltage-gating in voltage-gated potassium channels and their interaction with toxins from the venoms of poisonous animals. His work resulted in the first co-crystal structure of a potassium channel in complex with a pore-blocking toxin. Amongst other honors, Dr. Banerjee was the recipient of a Post Doctoral Fellowship from the Damon Runyon Cancer Research Foundation and was awarded the Nobel Laureate Signature Award for Graduate Education in Chemistry by the American Chemical Society.

The cell membrane is a uniquely complex and dynamic chemical environment. Even a simplistic binary description of an individual lipid molecule as hydrophobic tail and hydrophilic headgroup segments makes for a profoundly intricate environment considering the supramolecular ensemble of many such molecules that make up the membrane bilayer. Added to that are at least two facts that increase the chemical complexity of this environment - i) the cellular lipidome comprises of hundreds of lipid molecules whose spatiotemporal distribution is not static; ii) the membrane bilayer is juxtaposed adjacent to a rich aqueous phase with ions, small molecules and macromolecules ranging from small peptides to large proteins. Clearly, membrane proteins that have evolved to function in this milieu, have very different chemical properties and are governed by radically different constraints than soluble proteins.

The Banerjee lab is interested in the structural and chemical biology of membrane proteins. Their goal is to obtain detailed atomic descriptions of membrane proteins, to connect their structural chemistry with their cellular function in a healthy human being and to understand how structural and functional aberrations are linked to human diseases. Towards this end, they are combining structural tools such as crystallography and cryo EM, protein and peptide chemistry and functional assays using in vitro biochemical and biophysical techniques with detergent-solubilized proteins and reconstituted proteoliposomes. They are currently pursuing studies on membrane-embedded enzymes and transporters that move transition metal ions across the membrane.

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  • Eric Christenson, RN, BSN, CCRP
    Postdoctoral Fellow

  • Jin-sik Kim, RN, BSN, CCRP
    Postdoctoral Fellow

  • Chuljin Lee, RN, BSN, CCRP
    Postdoctoral Fellow

  • Robbins Puthenveetil, RN, BSN, CCRP
    Postdoctoral Fellow

  • Mitra Rana, RN, BSN, CCRP
    Postdoctoral Fellow

  • Grace Wang, RN, BSN, CCRP
    Post baccalaureate Fellow

  • 1) Christenson ET, Gallegos AS, Banerjee A (2018)
  • In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1
  • J. Biol. Chem., 293, 3819
  • 2) Rana M, Kumar P, Lee CJ, Verardi R, Rajashankar KR, Banerjee A (2018)
  • Fatty acyl recognition and transfer by an integral membrane S-acyltransferase
  • Science, 359, 6372
  • 3) Verardi R, Kim JS, Ghirlando R, Banerjee A. (2017)
  • Structural Basis for Substrate Recognition by the Ankyrin Repeat Domain of Human DHHC17 Palmitoyltransferase
  • Structure
  • 4) Banerjee A, Lee A, Campbell E, Mackinnon R. (2013)
  • Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel
  • Elife, 2:e00594
  • 5) 3. Qi Y, Spong MC, Nam K, Banerjee A, Jiralerspong S, Karplus M, Verdine GL (2009)
  • Encounter and extrusion of an intrahelical lesion by a DNA repair enzyme
  • Nature, 462(7274), 762-6
  • 6) Lee SY, Banerjee A, MacKinnon R. (2009)
  • Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels
  • PLoS Biol, 7(3), e47
  • 7) Banerjee A, Santos WL, Verdine GL (2006)
  • Structure of a DNA glycosylase searching for lesions
  • Science, 311(5764), 1153-7
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