« Previous AbstractGenetic and Structural Analyses of RRNPP Intercellular Peptide Signaling of Gram-Positive Bacteria    Next AbstractOdor-Active Compounds in the Special Flavor Hops Huell Melon and Polaris »

FEBS Lett

Title:		"A homology-based molecular model of the proline-rich homeodomain protein Prh, from haematopoietic cells"
Author(s):		Neidle S; Goodwin GH;
Address:		"CRC Biomolecular Structure Unit, Institute of Cancer Research, Sutton, Surrey, UK"
Journal Title:		FEBS Lett
Year:		1994
Volume:		345
Issue:		2-Mar
Page Number:		93 - 98
DOI:		10.1016/0014-5793(94)00446-3
ISSN/ISBN:		0014-5793 (Print) 0014-5793 (Linking)
Abstract:		"A molecular structural model for the homeodomain of the haematopoietic protein Prh together with its DNA recognition sequence, has been built using the known crystal structure of the MAT alpha 2 homeodomain as a starting-point. The modelling procedure used main and side-chain optimisations by means of molecular mechanics/simulated annealing procedures to obtain stereochemically plausible geometries. The resulting structure has a number of specific interactions in both major and minor grooves of the DNA that serve to define the consensus binding sequence for Prh. In particular, the side-chain of glutamine 50 is postulated to be involved in hydrogen bonds to adjacent adenine and cytosine bases within the consensus sequence"
Keywords:		"Amino Acid Sequence Animals DNA/metabolism DNA-Binding Proteins/biosynthesis/*chemistry/metabolism Drosophila/metabolism Erythrocytes/*metabolism Genes, Homeobox *Homeodomain Proteins Humans Mating Factor Models, Molecular Molecular Sequence Data Peptide;"
Notes:		"MedlineNeidle, S Goodwin, G H eng Comparative Study Research Support, Non-U.S. Gov't Review England 1994/05/30 FEBS Lett. 1994 May 30; 345(2-3):93-8. doi: 10.1016/0014-5793(94)00446-3"