至今,GenScript的服务及产品已被Cell, Nature, Science, PNAS等1300多家生物医药类杂志引用近万次,处于行业领先水平。NIH、哈佛、耶鲁、斯坦福、普林斯顿、杜克大学等约400家全球著名机构使用GenScript的基因合成、多肽服务、抗体服务和蛋白服务等成功地发表科研成果,再次证明GenScript 有能力帮助业内科学家Make research easy.

Molecular mechanism of interactions between ACAD9 and binding partners in mitochondrial respiratory complex I assembly

iScience. 2021-09; 
Chuanwu Xia, Baoying Lou, Zhuji Fu, Al-Walid Mohsen, Anna L Shen, Jerry Vockley, Jung-Ja P Kim
Products/Services Used Details Operation
DNA Sequencing … The N-terminal domain of ESCIT (Ser49-Ser269, which excludes the 48- GenScript (Piscataway, USA) residue mitochondrial targeting sequence and is hereafter referred to as N-ECSIT), and the C-terminal domain of ESCIT (Leu249-Ser431, referred to as C-ECSIT), were also … Get A Quote

摘要

The dual function protein ACAD9 catalyzes α,β-dehydrogenation of fatty acyl-CoA thioesters in fatty acid β-oxidation and is an essential chaperone for mitochondrial respiratory complex I (CI) assembly. ACAD9, ECSIT, and NDUFAF1 interact to form the core mitochondrial CI assembly complex. Current studies examine the molecular mechanism of ACAD9/ECSIT/NDUFAF1interactions. ACAD9 binds to the carboxy-terminal half and NDUFAF1 to the amino-terminal half of ECSIT. Binary complexes are unstable and aggregate easily, while the ACAD9/ECSIT/NDUFAF1 ternary complex is soluble and highly stable. Molecular modeling and small-angle X-ray scattering studies identified intra-complex interaction sites and binding sites for o... More

关键词

Biological sciences, Molecular biology, Structural biology