The Actin-Binding Prolyl-Isomerase Par17 Sustains Its Substrate Selectivity by Interdomain Allostery.

 0 Người đánh giá. Xếp hạng trung bình 0

Tác giả: Peter Bayer, Christine Beuck, Mike Blueggel, Jennifer Lynne Borger, Markus Kaiser, Bianca E Kamba, Farnusch Kaschani, Anja Matena, Anna Sternberg, Mathilda Thies

Ngôn ngữ: eng

Ký hiệu phân loại: 133.594 Types or schools of astrology originating in or associated with a

Thông tin xuất bản: United States : Proteins , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 698817

The human peptidyl-prolyl-cis/trans isomerases (PPIases), Parvulin 14 and Parvulin 17, accelerate the cis/trans isomerization of Xaa-Pro moieties within protein sequences. By modulating the respective binding interfaces of their target proteins, they play a crucial role in determining the fate of their substrates within the cell. Although both enzymes share the same amino acid sequence, they have different cellular functions. This difference is due to a 25 residue N-terminal extension present in Par17 but absent in Par14. Using activity assays, NMR spectroscopy, and mass spectrometry, we demonstrate that the N-terminal extension of Par17 determines substrate selectivity by an intramolecular allosteric mechanism and exhibits a target-binding motif that interacts with actin.
Tạo bộ sưu tập với mã QR

THƯ VIỆN - TRƯỜNG ĐẠI HỌC CÔNG NGHỆ TP.HCM

ĐT: (028) 36225755 | Email: tt.thuvien@hutech.edu.vn

Copyright @2024 THƯ VIỆN HUTECH