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Solution Structure of YKR049C, a Putative Redox Protein from Saccharomyces cerevisiae
Jung, Jin-Won,Yee, Adelinda,Wu, Bin,Arrowsmith, Cheryl H.,Lee, Weon-Tae Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.5
YKR049C is a mitochondrial protein in Saccharomyces cerevisiae that is conserved among yeast species, including Candida albicans. However, no biological function for YKR049C has been ascribed based on its primary sequence information. In the present study, NMR spectroscopy was used to determine the putative biological function of YKR049C based on its solution structure. YKR049C shows a well-defined thioredoxin fold with a unique insertion of helices between two $\beta$-strands. The central $\beta$-sheet divides the protein into two parts; a unique face and a conserved face. The 'unique face' is located between ${\beta}2$ and ${\beta}3$. Interestingly, the sequences most conserved among YKR049C families are found on this 'unique face', which incorporates L109 to E114. The side chains of these conserved residues interact with residues on the helical region with a stretch of hydrophobic surface. A putative active site composed by two short helices and a single Cys97 was also well observed. Our findings suggest that YKR049C is a redox protein with a thioredoxin fold containing a single active cysteine.
Structural Mapping of the C-terminal Domain of Human P73
지성욱,Ayeda Ayed,Petrer Yin,Cheryl Arrowsmith 한국자기공명학회 1998 Journal of the Korean Magnetic Resonance Society Vol.2 No.2
Human P37 is a recently-discovered homologue of the yumor suppressor P73. The location of its gene in chromosome 1 is deleted in many cancers, including colon and breast cancers, melanoma and neuroblastoma. 1 Its gene encodes two splice-variants, P73 - α and β, both exhibiting high sequence and structural similarity to P53, with an N - terminal transactivation domain, a central DNA-binding domain, and an oligomerization domain. 1 However P73 - α contains 136 extra residues in its C - terminus compared to the β variant, and 213 additional residues when compared to P53. since this domain is not present in P53 or the P73β variant, it may be important in defining a unique function for P73, or may function in modulating P53 - like functions of P73 through alternative oligomerization arrangements or interactions. Toward understanding the functional and/or structural role of this C - domain of P73α, we have begun NMR spectroscopic studies of several construct of the C - terminus, chosen using sequence alignments with two other proteins which also exhibit an extended C - terminus: rat KET protein, 2 and squid(Loligo forbesi) P53. 1,2 We report here the NMR characterization of several constructs of C – terminus of P73 and the identification of a small folded globular domain formed by residues 487 – 554. 영어논문