Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Academic Article uri icon

Overview

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.

publication date

  • March 1, 1997

Research

keywords

  • Hydrolases
  • Models, Structural
  • Protein Structure, Secondary
  • Proteins
  • UTP-Hexose-1-Phosphate Uridylyltransferase

Identity

PubMed Central ID

  • PMC2571075

Scopus Document Identifier

  • 0031051370

Digital Object Identifier (DOI)

  • 10.1038/nsb0397-231

PubMed ID

  • 9164465

Additional Document Info

volume

  • 4

issue

  • 3