Andrew Kruse

Assistant Professor of BCMP

SGM room 232A
250 Longwood Ave.
Boston, MA 02115
Tel: 617-432-3252

Lab Size: Between 5-10


G protein-coupled receptors (GPCRs) are cell-surface receptors that regulate neurotransmission, cardiovascular function, metabolic homeostasis, and many other physiological processes. Due to their central role in human physiology, these receptors are among the most important targets of therapeutic drugs, and are they among the most extensively studied proteins. To better understand GPCR signal transduction at a molecular level, we are using structural biology and biophysical methods to study model GPCRs such as muscarinic acetylcholine receptors. In addition, we are using new approaches in combinatorial biology to facilitate structural studies and to create protein ligands of GPCRs.

We are also interested in signal transduction pathways that remain less extensively studied than GPCRs, particularly receptors involved in the regulation of human metabolic homeostasis. In the long term, we hope to leverage our understanding of molecular signal transduction to guide the development of new and better therapeutics that modulate these pathways.



  1. Schmidt HR, Zheng S, Gurpinar E, Koehl A, Manglik A, Kruse AC. Crystal structure of the human sigma-1 receptor (2016) Nature 532 , 527-530.


  1. Kruse AC, Ring AM, Manglik A, Hu J, Hu K, Eitel K, Hübner H, Pardon E, Valant C, Sexton PM, Christopoulos A, Felder CC, Gmeiner P, Steyaert J, Weis WI, Garcia KC, Wess J, Kobilka BK. Activation and allosteric modulation of a muscarinic acetylcholine receptor. (2013) Nature 504, 101-106.


  1. Kruse AC, Weiss DR, Rossi M, Hu J, Hu K, Eitel K, Gmeiner P, Wess J, Kobilka BK, Shoichet BK. Muscarinic receptors as model targets and antitargets for structure-based ligand discovery. (2013) Mol. Pharm. 84, 528-540.


  1. Kruse AC, Hu J, Pan AC, Arlow DH, Rosenbaum DM, Rosemond E, Green HF, Liu T, Chae PS, Dror RO, Shaw DE, Weis WI, Wess J, Kobilka BK. Structure and dynamics of the M3 muscarinic acetylcholine receptor. (2012) Nature 482, 552-556.