https://repository.kopri.re.kr/handle/201206/5125 2026-04-07T05:40:33Z 2026-04-07T05:40:33Z Hyun-Woo Kim Myong Suk Yoo Kim, Hak Jun https://repository.kopri.re.kr/handle/201206/5951 2022-03-24T07:12:14Z 2007-01-01T00:00:00Z

Title: Characterization of a Myostatin-like Gene from the Scallop Patinopecten yessoensis Authors: Hyun-Woo Kim; Myong Suk Yoo; Kim, Hak Jun Abstract: Myostatin (GDF8) is a growth factor that limits muscle tissue growth and development in vertebrates. We isolated a myostatin-like gene (Py-MSTN) from the marine invertebrate the scallop Patinopecten yessoensis. Py-MSTN was highly expressed in the adductor muscle and in the gill unexpectedly. Amino acid analysis showed that Py-MSTN has 49% amino acid sequence identity and 64% similarity to human myostatin (Hs-MSTN), and 42% identity and 61% similarity to myoglianin, the only invertebrate homolog. These results indicated that Py-MSTN may be functionally similar to the vertebrate MSTN than the invertebrate homolog. Phylogenetic analysis suggested that Py-MSTN is an ancestral form of vertebrate MSTN and GDF11 and does not belong to other TGF-ß family members. Molecular modeling showed that Py-MSTN exhibits a similar tertiary structure to mammalian BMP7, a member of TGF-ß family. In addition, the amino acid residues which contact extracellular domain of the receptor were relatively conserved. Given these results, we propose that Py-MSTN is a functionally active member of the TGF-ß family and that it is involved in muscle growth and regulation.

2007-01-01T00:00:00Z Kim, Hak Jun https://repository.kopri.re.kr/handle/201206/7700 2022-03-24T07:13:16Z 2007-01-01T00:00:00Z

Title: Solution NMR Structure of Diacylglycerol Kinase (DAGK), A 40 kDa Integral Membrane Protein Authors: Kim, Hak Jun Abstract: Membrane proteins which comprise about 1/3 of the proteome play very important physiological roles in the cell. However compared to soluble counterparts, relatively feww membrane protein structures have been determined by any method. Structure determination of multi-span alpha-helical integral membrane proteins by NMR has been limited by the relatively poor spectral deispersion associated with their helical nature and difficulty in obtaining long-range distance restraints. Escherichia coli DAGK is a 40 kDa homotrimeric membrane protein composed of 121 residues. Each subunit has three transmembrane helices. DAGK catalyzes the phosphorylation of the lipid diacylglycerol by MgATP to phosphatidic acid and MgADP, and has served as a model system for membrane protein biocatalysis, stability and folding. To determine the structure of DAGK in detergent micelles, we have employed traditional chemical shift and NOE restraints, as well as paramagnetic relaxation enhancement (PRE) to obtain long-range distances. Here we present the NMR-derived structure of E. coli DAGK using long-range restraints obtained from paramagnetic relaxation enhancement combined with traditional restraints.

2007-01-01T00:00:00Z