Weird fingers: Functional analysis of WIP domain proteins

functional study of p0 proteins of two cereal yellow dwarf viruses (cydv-rpv and cydv-rps) and identification of their cellular partner

نقش سرکوبگری پروتئین p0 در دو پولروویروس کوتولگی زردی غلات cydv-rpv) و (cydv-rps، متفاوت در شدت بیماریزایی، مورد مطالعه قرار گرفت. نتایج نشان داد که هر دو پروتئین p0 p0cy-rpv) و (p0cy-rps قادر به سرکوب خاموشی آر ان ای ایجاد شده توسط ترادف های تراژن سنس و تکرار معکوس در n. benthamiana هستند. نشان داده شد که هر دو پروتئین p0 می توانند تخریب پروتئین argonaute-1 را تسهیل کنند. علاوه بر این، تمایل م...

Zinc Fingers Function Cooperatively with KRAB Domain for Nuclear Localization of KRAB-Containing Zinc Finger Proteins

Multiple nuclear localization domains have been identified in nuclear proteins, and they finely control nuclear import and functions of those proteins. ZNF268 is a typical KRAB-containing zinc finger protein (KRAB-ZFP), and previous studies have shown that the KRAB domain reinforces nuclear localization of KRAB-ZFPs by interacting with KAP1. In this study, we find that some of 24 zinc fingers o...

Nanobody as a new generation of functional proteins

Nanobody (Nb) or VHH is the smallest binding domain of camelid heavy chain antibody (HcAb). Light chains of HcAb naturally removed and because of some evolutionary changes, Nbs have unique properties rather than conventional antibodies. The size of Nb is about one-tenth (0.1) of whole antibodies and this size improved some problems of four chains antibodies such as high yield of expression in p...

GRP2 proteins contain both CCHC zinc fingers and a cold shock domain.

Peripheral membrane proteins: FYVE sticky fingers

The recently determined structure of the lipid-binding 'FYVE' domain provides several clues to the mode of interaction for this class of peripheral membrane proteins. However, the application of traditional modes of structural analysis to diffusible membrane-binding proteins exposes some limitations of these techniques.