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Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1508-13. Epub 2005 Oct 19.

Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase.

Author information

1
Department of Molecular Sciences, University of Tennessee Health Science Center, USA.

Abstract

The crystal structure of human liver glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been determined. This structure represents the first moderate-resolution (2.5 A) 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.

PMID:
16239728
DOI:
10.1107/S0907444905026740
[Indexed for MEDLINE]

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