Linked Life Data

17713798

Source:http://linkedlifedata.com/resource/pubmed/id/17713798

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2007-9-17
pubmed:abstractText
S100B protein is one of the factors involved in the down-regulation of tumor suppressor protein p53, a transcription activator that signals for cycle arrest and apoptosis. As the inactivation of normal p53 functions is found in over half of human cancers, restoration of normal p53 functions through the destruction or prevention of S100B--p53 complexes represents a possible approach for the development of anti-cancer drugs. The aim of this work was to propose the S100B binding interface through an examination of the literature and use of molecular modeling (MM) techniques with AutoDock program and the AMBER force field. We propose two residues in the S100B binding pocket (Val56, Phe76) and two residues on the protein surface (Val52, Ala83) are essential for ligand binding. The data presented here indicate that interactions with these four residues are necessary for a reduction in the incidence of the S100B--p53 complex. Additionally, we have tried to explain a mechanism for the action of pentamidine, the best-known S100B ligand, and have proposed two S100B--pentamidine structures. The results presented here may be useful for the efficient design of new S100B ligands.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0948-5023
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1123-31
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Theoretical study on binding of S100B protein.
pubmed:affiliation
Protera S. r. l., Viale delle Idee, 22, 50019, Sesto Fiorentino, Fi, Italy. gieldon@proterasrl.com
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't