In silico study of fragile histidine triad interaction domains with MDM2 and p53.

ABSTRACT:

Background

Fragile histidine triad (FHIT) is considered as a member of the histidine triad (HIT) nucleotide-binding protein superfamily regarded as a putative tumor suppressor executing crucial role in inhibiting p53 degradation by MDM2. Accumulating evidences indicate FHIT interaction with p53 or MDM2; however, there is no certain study deciphering functional domains of FHIT involving in the interaction with MDM2 and/or p53. In this regard, such evident interaction can spring in mind determining important domains of FHIT binding to MDM2 with regard to p53.

Materials and methods

Since there were not any previous studies appraising complete three-dimensional structures of target molecules, molecular modeling was carried out to construct three-dimensional models of full FHIT,

SUBMITTER: Eslamparast A 

PROVIDER: S-EPMC4162077 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature