Journal article
Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins
Nature Structural Biology, Vol.4(3), pp.231-238
03/1997
DOI: 10.1038/nsb0397-231
PMID: 9164465
Abstract
Histidine triad nucleotide-binding protein (HINT), a dimeric purine nucleotide-binding protein from rabbit heart, is a member of the HIT (histidine triad) superfamily which includes HINT homologues and FHIT (HIT protein encoded at the chromosome 3 fragile site) homologues. Crystal structures of HINT-nucleotide complexes demonstrate that the most conserved residues in the superfamily mediate nucleotide binding and that the HIT motif forms part of the phosphate binding loop. Galactose-1-phosphate uridylyltransferase, whose deficiency causes galactosemia, contains tandem HINT domains with the same fold and mode of nucleotide binding as HINT despite having no overall sequence similarity. Features of FHIT, a diadenosine polyphosphate hydrolase and candidate tumour suppressor, are predicted from HINT-nucleotide structures.
Details
- Title: Subtitle
- Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins
- Creators
- Charles BrennerPreston GarrisonJeffrey GilmourDaniel PeisachDagmar RingeGregory A PetskoJohn M Lowenstein
- Resource Type
- Journal article
- Publication Details
- Nature Structural Biology, Vol.4(3), pp.231-238
- DOI
- 10.1038/nsb0397-231
- PMID
- 9164465
- NLM abbreviation
- Nat Struct Biol
- ISSN
- 1072-8368
- eISSN
- 2331-365X
- Language
- English
- Date published
- 03/1997
- Academic Unit
- Biochemistry and Molecular Biology; Internal Medicine
- Record Identifier
- 9983788599202771
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