Vasanthi Jayaraman, Ph.D.

Professor and Co-Director
BMB Graduate Program

Description of Research


Communication between nerve cells serves as the basis of all brain activity, and one of the fundamental steps involved in signal transmission between the nerve cells, is the conversion of a “chemical” signal liberated at the end of one nerve cell, into an “electrical” signal at the second nerve cell. This step is mediated by a class of membrane bound proteins known as neurotransmitter receptors. Glutamate receptors belong to this family of proteins, and are the main excitatory receptors in the central nervous system.

Our laboratory is interested in gaining an understanding of agonist mediated activation and desensitization of this receptor by determining the structural changes in the protein induced by agonist binding. This is achieved by using various cutting edge spectroscopic methods that allow the characterization of the dynamic state structure of the proteins at a significantly higher resolution than X-ray structures. The structural changes thus determined are correlated to the functional consequences as measured by electrophysiological measurements. These investigations provide a detailed understanding of the agonist controlled function of the glutamate receptors and hence aid in the rational design of drugs targeting this group of important proteins that are involved in diverse neuropathologies, such as epilepsy and ischemia.


Contact Information

UTHealth Medical School
Department of Biochemistry and Molecular Biology
6431 Fannin Street, MSB 6.174
Houston, Texas 77030

713-500-6236 Direct  713-500-0652 Fax


PhD - Princeton University

Postdoctoral Fellow - Cornell University

Research Interests

Structure and function of Membrane proteins , Ligand gated ion channels


Amino-terminal Domain Tetramer Organization and Structural Effects of Zinc Binding in the N-Methyl-D-aspartate (NMDA) Receptor.

Sirrieh RE, Maclean DM, Jayaraman V.

J Biol Chem. 2013 Aug 2;288(31):22555-64. doi: 10.1074/jbc.M113.482356. Epub 2013 Jun 21.

PMID: 23792960

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Role of conformational dynamics in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor partial agonism.

Ramaswamy S, Cooper D, Poddar N, MacLean DM, Rambhadran A, Taylor JN, Uhm H, Landes CF,Jayaraman V.

J Biol Chem. 2012 Dec 21;287(52):43557-64. doi: 10.1074/jbc.M112.371815. Epub 2012 Oct 31.

PMID: 23115239

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Structural landscape of isolated agonist-binding domains from single AMPA receptors.

Landes CF, Rambhadran A, Taylor JN, Salatan F, Jayaraman V.

Nat Chem Biol. 2011 Mar;7(3):168-73. doi: 10.1038/nchembio.523. Epub 2011 Feb 6.

PMID: 21297640

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