مطالعه In silico دومینهای تداخلی FHIT با MDM2 و p53

اسلام پرست, آمنه ، سرداری, سروش ، قهرمانی, محمدحسین (1393) مطالعه In silico دومینهای تداخلی FHIT با MDM2 و p53. Advanced Biomedical Research ــ 3 (1). ص.ص.1-7. شاپا 2277-9175

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آدرس اینترنتی رسمی : http://www.advbiores.net/article.asp?issn=2277-917...

عنوان انگليسي

In silico study of FHIT interaction domains with MDM2 and p53

خلاصه انگلیسی

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, MDM2, P53 and also FHIT segments. Truncated structures of FHIT were created to reveal critical regions engaging in FHIT interaction. Results: Given the shape and shape/electrostatic total energy, FHIT structures (β1-5), (β3-7, α1), and (β5-7, α1) appeared to be better candidates than other structures in interaction with full MDM2. Furthermore, FHIT structures (β6-7), (β6-7, α1), (β4-7, α1) were considered to be better than other structures in interaction with p53. FHIT truncates that interact with MDM2 presented lower energy levels than FHIT truncates interacting with p53. Conclusion: These findings are beneficial to understand the mechanism of the FHIT-MDM2-p53 complex activation for designing inhibitory compounds.

نوع سند :مقاله
زبان سند : انگلیسی
نویسنده اول :آمنه اسلام پرست
نویسنده مسئول :سروش سرداری
استاد راهنما :محمدحسین قهرمانی
اطلاعات اضافی :Indexing Information : PubMed, Pubmed Central, EBSCO Publishing's Electronic Databases, Expanded Academic ASAP, Genamics JournalSeek, Global Health, Google Scholar, Hinari, Index Copernicus, MANTIS, National Science Library, OpenJGate, PrimoCentral, ProQuest, SCOLOAR, SIIC databases, Summon by Serial Solutions and Ulrich's International Periodical Directory
کلید واژه ها (انگلیسی):Bioinformatics, fragile histidine triad, functional domains, tumor suppressor
موضوعات :QV فارماکولوژی > QV 737 بیوتکنولوژی دارویی
بخش های دانشگاهی :دانشکده داروسازی > بخش بیوتکنولوژی دارویی
کد شناسایی :6034
ارائه شده توسط : دکتر آمنه اسلام پرست
ارائه شده در تاریخ :15 آبان 1393 08:48
آخرین تغییر :15 آبان 1393 08:48

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