잠시만 기다려 주세요. 로딩중입니다.

Crystal Structure of p97-N/D1 Hexamer Complexed with FAF1 UBX Domain

Journal of the Korean Chemical Society 2023년 67권 5호 p.348 ~ 352
강원철,
소속 상세정보
강원철 ( Kang Won-Chull ) 

Abstract


p97, a universally conserved AAA+ ATPase, holds a central position in the ubiquitin-proteasome system, orchestrating myriad cellular activities with significant therapeutic implications. This protein primarily interacts with a diverse set of adaptor proteins through its N-terminal domain (NTD), which is structurally located at the periphery of the D1 hexamer ring. While there have been numerous structural elucidations of p97 complexed with adaptor proteins, the stoichiometry has remained elusive. In this work, we present the crystal structure of the p97-N/D1 hexamer bound to the FAF1-UBX domain at a resolution of 3.1 A. Our findings reveal a 6:6 stoichiometry between the p97 hexamer and FAF1-UBX domain, deepening our understanding from preceding structural studies related to p97-NTD and UBX domain-containing proteins. These insights lay the groundwork for potential therapeutic interventions addressing cancer and neurodegenerative diseases.

키워드

p97; valosin-containing protein; Fas-associated factor 1; Ubiquitin regulatory X, UBX

원문 및 링크아웃 정보

등재저널 정보