Structure of the PAPP-ABP5 complex reveals mechanism of substrate recognition
PAPP-A substrate selectivity underlies the tight regulation of IGF signaling. Here, the authors report cryo-EM structures of dimeric PAPP-A in its substrate-free form and in complex with a peptide substrate, which combined with biochemical assays provide a mechanism for PAPP-A substrate binding and...
Main Authors: | Russell A. Judge, Janani Sridar, Kathryn Tunyasunvunakool, Rinku Jain, John C. K. Wang, Christna Ouch, Jun Xu, Amirhossein Mafi, Aaron H. Nile, Clint Remarcik, Corey L. Smith, Crystal Ghosh, Chen Xu, Vincent Stoll, John Jumper, Amoolya H. Singh, Dan Eaton, Qi Hao |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2022-09-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-022-33175-2 |
Similar Items
-
Author Correction: Structure of the PAPP-ABP5 complex reveals mechanism of substrate recognition
by: Russell A. Judge, et al.
Published: (2022-09-01) -
Cryo-EM structure of human PAPP-A2 and mechanism of substrate recognition
by: Janani Sridar, et al.
Published: (2023-10-01) -
PPG2ABP: Translating Photoplethysmogram (PPG) Signals to Arterial Blood Pressure (ABP) Waveforms
by: Nabil Ibtehaz, et al.
Published: (2022-11-01) -
G. Papp Katalin: Győr utcanevei
by: Erzsébet Erdélyi
Published: (2007-12-01) -
¿Qué es el ABP?
by: Patricio Barzallo
Published: (2019-06-01)