프탈이미드 유도체를 이용한 알칼리 세정성 분산염료의 합성 및 염색성에 관한 연구

학위논문(석사)--서울대학교 대학원 :섬유고분자공학과,1997.Maste

플루오르술폰기를 갖는 알칼리 세정성 아조계 분산 염료의 합성, 응용 및 가수분해의 반응속도론적 고찰

Thesis (doctoral)--서울대학교 대학원 :재료공학부,2002.Docto

A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein

The cAMP receptor protein (CRP) of Escherichia coli exists in an equilibrium between active and inactive forms, and the effector, cAMP, shifts that equilibrium to the active form, thereby allowing DNA binding. For this equilibrium shift, a C-helix repositioning around the C-helix residues Thr-127 and Ser-128 has been reported as a critical local event along with proper β4/β5 positioning. Here we show that another C-helix residue, Arg-123, has a unique role in cAMP-dependent CRP activation in two different ways. First, Arg-123 is important for proper cAMP affinity, although it is not critical for the conformational change with saturating amounts of cAMP. Second, Arg-123 is optimal for stabilizing the inactive conformation of CRP when cAMP is absent, thereby allowing a maximal range of regulation by cAMP. However, Arg-123 does not appear to be critical for a functional response to cAMP, as has been proposed previously (Berman, H. M., Ten Eyck, L. F., Goodsell, D. S., Haste, N. M., Korney, A., and Taylor, S. S. (2005) Proc. Natl. Acad. Sci. U. S. A. 102, 45-50). Based on mutagenic evidence, we also propose the basis for the stabilization of the inactive form to be through a salt interaction between Asp-68 and Arg-123. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.OAIID:RECH_ACHV_DSTSH_NO:T200700352RECH_ACHV_FG:RR00200001ADJUST_YN:EMP_ID:A080565CITE_RATE:5.581DEPT_NM:생명과학부EMAIL:[email protected]_YN:YY