faculty

William N. Zagotta

zagotta@uw.edu

University of Washington, 

Biophysical and Structural Biology

Neuroscience

Molecular mechanisms of ion channel function

Faculty Contact Information

Building: Health Sciences Building Room: K551 Box: 357290 Phone: 206-685-3878

Lab Information

Location: University of Washington Medical Center Building: Health Sciences Building Room: K563 Box: 357290 Phone: 206-543-3598 Alt Phone: (206) 685-8076 http://depts.washington.edu/pbiopage/faculty/wzagotta

Accepting Students For:

Rotation, Spring
Permanent

Publications

Insights into the molecular mechanism for hyperpolarization-dependent activation of HCN channels.

Flynn GE, Zagotta WN.

Proceedings of the National Academy of Sciences of the United States of America. 2018; 115(34):E8086-E8095.

PubMed [journal]
PMID:
30076228
PMCID:
PMC6112743

Visualizing conformational dynamics of proteins in solution and at the cell membrane.

Gordon SE, Munari M, Zagotta WN.

eLife. 2018; 7.

PubMed [journal]
PMID:
29923827
PMCID:
PMC6056233

Dynamic rearrangement of the intrinsic ligand regulates KCNH potassium channels.

Dai G, James ZM, Zagotta WN.

The Journal of general physiology. 2018; 150(4):625-635.

PubMed [journal]
PMID:
29567795
PMCID:
PMC5881448

Structural insights into the mechanisms of CNBD channel function.

James ZM, Zagotta WN.

The Journal of general physiology. 2018; 150(2):225-244.

PubMed [journal]
PMID:
29233886
PMCID:
PMC5806680

The Therapeutic Antibody LM609 Selectively Inhibits Ligand Binding to Human αVβ3 Integrin via Steric Hindrance.

Borst AJ, James ZM, Zagotta WN, Ginsberg M, Rey FA, DiMaio F, Backovic M, Veesler D.

Structure (London, England : 1993). 2017; 25(11):1732-1739.e5. NIHMSID: NIHMS912485

PubMed [journal]
PMID:
29033288
PMCID:
PMC5689087

Research Summary

Our goal is to determine the molecular mechanisms of the opening and closing conformational changes in ion channels. We focus on a family of channels that is regulated by the direct binding of cyclic nucleotides, cAMP and cGMP. These channels are important for sensory transduction, and in the control of pacemaker activity in the heart. We employ a variety of approaches including electrophysiology, site-directed mutagenesis, fluorescence spectroscopy, and X-ray crystallography. By the combination of these approaches we gain new insights into the molecular mechanisms for channel function.