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Titolo:
A HOMOLOGY-BASED MOLECULAR-MODEL OF THE PROLINE-RICH HOMEODOMAIN PROTEIN PRH, FROM HEMATOPOIETIC-CELLS
Autore:
NEIDLE S; GOODWIN GH;
Indirizzi:
INST CANC RES,CRC,BIOMOLEC STRUCT UNIT,COTSWOLD RD SUTTON SM2 5NG SURREY ENGLAND INST CANC RES,CHESTER BEATTY LABS LONDON SW3 6JB ENGLAND
Titolo Testata:
FEBS letters
fascicolo: 2-3, volume: 345, anno: 1994,
pagine: 93 - 98
SICI:
0014-5793(1994)345:2-3<93:AHMOTP>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
DNA-BINDING SPECIFICITY; HEMATOPOIETIC LINEAGES; CRYSTAL-STRUCTURE; GENE; COMPLEX; SPECTROSCOPY; RECOGNITION;
Keywords:
PRH PROTEIN; HOMEODOMAIN; MOLECULAR MODELING; PROTEIN-DNA RECOGNITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
S. Neidle e G.H. Goodwin, "A HOMOLOGY-BASED MOLECULAR-MODEL OF THE PROLINE-RICH HOMEODOMAIN PROTEIN PRH, FROM HEMATOPOIETIC-CELLS", FEBS letters, 345(2-3), 1994, pp. 93-98

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 asa 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 sequencefor 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 12:10:39