상길! 홈페이지 상길이를 만나요| ZanNavi's space
  현재위치 ► ZanNavi's space : iBib : Abstract  

----------------------------------------------------------------------
iBib | list | admin

Abstract of [Myllykoski12]

[Myllykoski12]
Download a PDF: 2Mb

Myelin 2',3'-cyclic nucleotide 3'-phosphodiesterase: Active-site ligand binding and molecular conformation

Matti Myllykoski, Arne Raasakka, Huijong Han, and Petri Kursula

PLoS ONE 7, e32336 (2012)

[bib][BibTeX][pdf][pdf][link]doi:10.1371/journal.pone.0032336

The 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) is a highly abundant membrane-associated enzyme in the myelin sheath of the vertebrate nervous system. CNPase is a member of the 2H phosphoesterase family and catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates; however, its physiological substrate and function remain unknown. It is likely that CNPase participates in RNA metabolism in the myelinating cell. We solved crystal structures of the phosphodiesterase domain of mouse CNPase, showing the binding mode of nucleotide ligands in the active site. The binding mode of the product 2'-AMP provides a detailed view of the reaction mechanism. Comparisons of CNPase crystal structures highlight flexible loops, which could play roles in substrate recognition; large differences in the active-site vicinity are observed when comparing more distant members of the 2H family. We also studied the full-length CNPase, showing its N-terminal domain is involved in RNA binding and dimerization. Our results provide a detailed picture of the CNPase active site during its catalytic cycle, and suggest a specific function for the previously uncharacterized N-terminal domain.

Tags: CSSB-HZI, DESY, CNPase


made by ZN

----------------------------------------------------------------------

이 페이지의 최종수정일: 2021.2.2
Copyright (C) 2000-2024 손상길
저작권에 대한 본 사항이 명시되는 한, 어떠한 정보 매체에 의한 본문의 전재나 발췌도 무상으로 허용됩니다. [copyleft]