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Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase
- Source :
- Acta Crystallographica Section D Biological Crystallography. 61:1508-1513
- Publication Year :
- 2005
- Publisher :
- International Union of Crystallography (IUCr), 2005.
-
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.
- Subjects :
- Models, Molecular
Trypanosoma
Protein Conformation
Protein subunit
Dehydrogenase
Nicotinamide adenine dinucleotide
Crystallography, X-Ray
Structure-Activity Relationship
chemistry.chemical_compound
Protein structure
stomatognathic system
Trypanosomiasis
Structural Biology
Animals
Humans
Enzyme Inhibitors
Muscle, Skeletal
Glyceraldehyde 3-phosphate dehydrogenase
chemistry.chemical_classification
biology
Glyceraldehyde-3-Phosphate Dehydrogenases
Parkinson Disease
General Medicine
Molecular biology
Enzyme
Liver
chemistry
Biochemistry
Drug Design
biology.protein
NAD+ kinase
Homotetramer
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 61
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section D Biological Crystallography
- Accession number :
- edsair.doi.dedup.....b3375f2d3779168526e73447d8310921