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David Ortiz
Baylor College of Medicine and PNRIDepartment: SCBMBAddress: Pacific Northwest Research Institute 720 Broadway Seattle, WA 98122 Phone: (206) 726-1200 Fax: Email: do148010@bcm.tmc.edu Web: |
Education
B.S. Mathematics, UT-Austin (2000)
Mentor:
Wah Chiu, Ph.D.
Joseph Bryan, Ph.D.
Honors
HAMBP Pre-doctoral Fellow 2005-2007
NSF GK-12 Fellow 2006-2007
GRC Travel Award 2006
ASBMB Travel Award 2008
Research Topic
Pharmacology and Enzymology of the Sulfonylurea Receptor
Research Description
Sulfonylurea receptors (SUR) are members of the ATP-binding cassette (ABC) superfamily, which usually transport a wide variety of substrates both into and out of cells using energy from ATP-hydrolysis. SURs are unusual among ABC proteins in that they currently have no known transport substrate and use the motion derived from ATP binding and/or hydrolysis to regulate an associated ion channel. The full complex, known as the ATP-sensitive potassium (KATP) channel is a heteroctamer composed of a potassium inward rectifier (KIR6.x) and SUR in a 4:4 stoichiometry. The neuroendocrine isoform (SUR1/KIR6.2) mediates insulin release from pancreatic beta cells and a major class of anti-diabetic drugs, sulfonylureas (i.e. glibenclamide) stimulates insulin release by binding to SUR1 and closing KATP. My research focuses on three major questions. How does the hydrolytic cycle of SUR1 correspond to the activity of the KATP channel (i.e. which enzymatic intermediates of SUR1 open/close the channel)? How do KATP agonists/antagonists that bind to SUR1 modulate its ATPase activity? How do disease causing mutations in SUR1 effect both its drug binding and enzymatic properties?
Selected Publications
- Little JB, Ortiz D, Ortiz-Rosado R, Pablo R, Rios-Soto K. Some remarks on Fitzpatrick and Flynn's Grobner basis technique for Pade approximation. J. Symb. Comput. 35(4): 451-461 (2003)
Last edited on: September 10, 2009