Picture of Andrew Kruse

Andrew Kruse, Ph.D.

Professor of Biological Chemistry and Molecular Pharmacology

Our research aims to elucidate the molecular basis of membrane protein signaling using techniques including protein engineering, structural biology, and pharmacology.

Research:

Signal transduction across cell membranes plays a central role in human physiology and disease, yet the mechanistic details underlying transmembrane signaling remain poorly understood. Our research aims to elucidate the molecular basis of membrane protein signaling using techniques including protein engineering, structural biology, and pharmacology. In particular, we are focused on the study of proteins important in human health and disease, including G protein-coupled receptors and other proteins that regulate neurotransmission and metabolic homeostasis.

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.

Address: 

Room SGM - 227

250 Longwood Avenue

Boston, MA 02115

Publications View
Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins.
Authors: Authors: Chae PS, Rasmussen SG, Rana RR, Gotfryd K, Chandra R, Goren MA, Kruse AC, Nurva S, Loland CJ, Pierre Y, Drew D, Popot JL, Picot D, Fox BG, Guan L, Gether U, Byrne B, Kobilka B, Gellman SH.
Nat Methods
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Negative selection and peptide chemistry determine the size of naive foreign peptide-MHC class II-specific CD4+ T cell populations.
Authors: Authors: Chu HH, Moon JJ, Kruse AC, Pepper M, Jenkins MK.
J Immunol
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Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms.
Authors: Authors: Huseby MJ, Kruse AC, Digre J, Kohler PL, Vocke JA, Mann EE, Bayles KW, Bohach GA, Schlievert PM, Ohlendorf DH, Earhart CA.
Proc Natl Acad Sci U S A
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X-ray crystallographic analysis of adipocyte fatty acid binding protein (aP2) modified with 4-hydroxy-2-nonenal.
Authors: Authors: Hellberg K, Grimsrud PA, Kruse AC, Banaszak LJ, Ohlendorf DH, Bernlohr DA.
Protein Sci
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Identification and characterization of a small molecule inhibitor of Fatty Acid binding proteins.
Authors: Authors: Hertzel AV, Hellberg K, Reynolds JM, Kruse AC, Juhlmann BE, Smith AJ, Sanders MA, Ohlendorf DH, Suttles J, Bernlohr DA.
J Med Chem
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Reduced ability of C-type natriuretic peptide (CNP) to activate natriuretic peptide receptor B (NPR-B) causes dwarfism in lbab -/- mice.
Authors: Authors: Yoder AR, Kruse AC, Earhart CA, Ohlendorf DH, Potter LR.
Peptides
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