Ismail, S.A. and Park, H.W. (2005) Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallographica Section D: Biological Crystallography, 61(11), pp. 1508-1513. (doi: 10.1107/S0907444905026740) (PMID:16239728)
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Abstract
The crystal structure of human liver glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been determined. This structure represents the first moderate-resolution (2.5 Å) and crystallographically refined (Rfree = 22.9%) human GAPDH structure. The liver GAPDH structure consists of a homotetramer, each subunit of which is bound to a nicotinamide adenine dinucleotide (NAD+) molecule. The GAPDH enzyme has glycolytic and non-glycolytic functions, both of which are of chemotherapeutic interest. The availability of a high-quality human GAPDH structure is a necessity for structure-based drug design. In this study, structural differences between human liver and skeletal muscle GAPDHs are reported in order to understand how these two enzymes might respond to anti-trypanosomatid GAPDH inhibitors.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Ismail, Dr Shehab |
| Authors: | Ismail, S.A., and Park, H.W. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Cancer Sciences |
| Journal Name: | Acta Crystallographica Section D: Biological Crystallography |
| Publisher: | International Union of Crystallography |
| ISSN: | 0907-4449 |
| ISSN (Online): | 1399-0047 |
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