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International Journal of Medicinal Chemistry
Volume 2018, Article ID 9419521, 21 pages
Review Article

Crystallography and Its Impact on Carbonic Anhydrase Research

University of Florida College of Medicine, Department of Biochemistry and Molecular Biology, Gainesville, FL 32610, USA

Correspondence should be addressed to Robert McKenna; ude.lfu@annekcmr

Received 2 May 2018; Accepted 16 August 2018; Published 13 September 2018

Academic Editor: Qi-Dong You

Copyright © 2018 Carrie L. Lomelino et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


X-ray and neutron crystallography are powerful techniques utilized to study the structures of biomolecules. Visualization of enzymes in complex with substrate/product and the capture of intermediate states can be related to activity to facilitate understanding of the catalytic mechanism. Subsequent analysis of small molecule binding within the enzyme active site provides insight into mechanisms of inhibition, supporting the design of novel inhibitors using a structure-guided approach. The first X-ray crystal structures were determined for small, ubiquitous enzymes such as carbonic anhydrase (CA). CAs are a family of zinc metalloenzymes that catalyze the hydration of CO2, producing and a proton. The CA structure and ping-pong mechanism have been extensively studied and are well understood. Though the function of CA plays an important role in a variety of physiological functions, CA has also been associated with diseases such as glaucoma, edema, epilepsy, obesity, and cancer and is therefore recognized as a drug target. In this review, a brief history of crystallography and its impact on CA research is discussed.