Epernicus: Michael A Hast, B.Sc.

Michael A Hast, B.Sc.

Position:
Graduate Student - Ph.D.

Biochemistry

Structural Biology and Biophysics

Duke University (Durham, NC)
Advisor:
Lorena s Beese
Degrees:

B.Sc., Biochemistry, North Carolina State University (Raleigh, NC)
Past Advisors:
Research:
Structural enzymology of protein prenyltransferases

Structure determination of protein prenyltransferases from human pathogens (such as Candida albicans, Cryptococcus neoformans, and Trypanosoma brucei) using X-ray crystallography. The prenyltransferases from these organisms are expected to be good drug targets, and we are looking to elucidate the structural determinants of substrate and inhibitor binding for the purposes of designing new antiparasitic agents.

Communities:

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Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase.
Hast MA, Fletcher S, Cummings CG, Pusateri EE, Blaskovich MA, Rivas K, Gelb MH, Van Voorhis WC, Sebti SM, Hamilton AD, Beese LS

Chemistry & biology. 2009 Feb 27;16(2):181-92
Caged protein prenyltransferase substrates: tools for understanding protein prenylation.
DeGraw AJ, Hast MA, Xu J, Mullen D, Beese LS, Barany G, Distefano MD

Chemical biology & drug design. 2008 Sep;72(3):171-81
Structure of protein geranylgeranyltransferase-I from the human pathogen Candida albicans complexed with a lipid substrate.
Hast MA, Beese LS

The Journal of biological chemistry. 2008 Aug 19
Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase.
Eastman RT, White J, Hucke O, Yokoyama K, Verlinde CL, Hast MA, Beese LS, Gelb MH, Rathod PK, Van Voorhis WC

Molecular and biochemical parasitology. 2007 Mar;152(1):66-71

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