6RHN

HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT WITHOUT NUCLEOTIDE

6RHN の概要

• エントリーDOI: 10.2210/pdb6rhn/pdb
• 分子名称: HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (2 entities in total)
• 機能のキーワード: nucleotide-binding protein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Cytoplasm: P80912
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12584.53

構造登録者

Brenner, C.,Garrison, P.,Gilmour, J.,Peisach, D.,Ringe, D.,Petsko, G.A.,Lowenstein, J.M. (登録日: 1997-02-27, 公開日: 1997-06-16, 最終更新日: 2024-05-22)

主引用文献

Brenner, C.,Garrison, P.,Gilmour, J.,Peisach, D.,Ringe, D.,Petsko, G.A.,Lowenstein, J.M.
Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.
Nat.Struct.Biol., 4:231-238, 1997

PubMed 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.

PubMed: 9164465
DOI: 10.1038/nsb0397-231

実験手法

X-RAY DIFFRACTION (2.15 Å)