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A homology‐based molecular model of the proline‐rich homeodomain protein Prh, from haematopoietic cells
Author(s) -
Neidle Stephen,
Goodwin Graham H.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00446-3
Subject(s) - homeobox , cytosine , dna , computational biology , chemistry , biology , genetics , biochemistry , gene , gene expression
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 MATα2 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.