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

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Ismail SA, Park HW

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

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

PubMed ID

16239728 [ View in PubMed

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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 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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
NADH	Glyceraldehyde-3-phosphate dehydrogenase, testis-specific	Protein	Humans	Unknown	Not Available	Details

Polypeptides

Name	UniProt ID
Glyceraldehyde-3-phosphate dehydrogenase	P04406	Details