Abstract
PDZ 도메인을 통하여 여러 단백질과 상호작용하며 신경전달 기전에 관여하는 단백질로 Shank1, Shank2, Shank3, PDS-95, AF있다. 본 연구는 Shank3 PDZ 도메인의 구조를 밝히기 위한 첫 단계로서 Shank3 단백질의 PDZ 도메인을 동정하였고, E. coli에서 발현하여 생성된 단백질을 정제한 후 1차 NMR 구조분석을 시도하였다. 그 결과에 의하면 정제된 Shank3 PDZ 단백질은 순도가 높고 안정적인 접힘(folding)구조를 제시하고있다. 현재 완전한 NMR 구조분석을 위해 좀더 많은 양의 정제된 Shank3 PDZ 단백질을 얻고자 연구하고 있다. We wished to create a set of small molecular weight PDZ domain ligands that may be used in functional studies on the proteins AF6, PSD-95 and Shank. As a starting point, the Shank3 PDZ domain was cloned, purified, and characterized the structure of Shank3 PDZ domain by 1D <TEX>$^1H-NMR$</TEX>. The chemical shift dispersion of the proton signals indicates that the purified Shank3 PDZ protein is very pure and globally well folded. Currently, we are working on improving the yield of the protein production for complete NMR structural analysis of the Shank3 PDZ domain.
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