The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain.

Détails

ID Serval
serval:BIB_2060CFCBC6F3
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain.
Périodique
Cell
Auteur(s)
Assa-Munt N., Mortishire-Smith R.J., Aurora R., Herr W., Wright P.E.
ISSN
0092-8674[print], 0092-8674[linking]
Statut éditorial
Publié
Date de publication
04/1993
Volume
73
Numéro
1
Pages
193-205
Langue
anglais
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Résumé
The POU-specific (POUs) domain, in association with a POU-type homeodomain, forms the bipartite DNA-binding POU domain. The solution structure of the Oct-1 POUs domain has been determined by multidimensional nuclear magnetic resonance spectroscopy and consists of four alpha helices surrounding a conserved hydrophobic core. The POUs domain is structurally similar to the DNA-binding domains of the bacteriophage lambda and 434 repressors and 434 Cro. These domains exhibit superimposable helix-turn-helix (HTH) motifs, except that in the POUs domain, the first helix and the linker to the second helix of the motif are extended. The conserved structural features have been used to propose a plausible model for DNA binding by the POUs domain. A human dwarfism mutation that affects positive control in the related POU domain protein Pit-1 maps to the same region of the HTH motif as do positive control mutations in lambda repressor.
Mots-clé
Amino Acid Sequence, Bacteriophage lambda, Base Sequence, Computer Graphics, DNA-Binding Proteins/chemistry, Host Cell Factor C1, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Octamer Transcription Factor-1, POU Domain Factors, Protein Structure, Tertiary, Repressor Proteins/chemistry, Sequence Homology, Amino Acid, Solutions, Structure-Activity Relationship, Transcription Factors/chemistry, Viral Proteins, Viral Regulatory and Accessory Proteins
Pubmed
Web of science
Création de la notice
24/01/2008 15:36
Dernière modification de la notice
20/08/2019 12:56
Données d'usage