Structural dynamics of the active HER4 and HER2/HER4 complexes is finely tuned by different growth factors and glycosylation

Autor: Raphael Trenker, Devan Diwanji, Tanner Bingham, Kliment A Verba, Natalia Jura

Publikováno v: eLife, Vol 12 (2024)

Human Epidermal growth factor Receptor 4 (HER4 or ERBB4) carries out essential functions in the development and maintenance of the cardiovascular and nervous systems. HER4 activation is regulated by a diverse group of extracellular ligands including

Externí odkaz: https://doaj.org/article/bc19c740093f48b8a2cb5fc7b76488b3

Structures of the HER2–HER3–NRG1β complex reveal a dynamic dimer interface

Autor: Natalia Jura, Devan Diwanji, Tarjani M. Thaker, Raphael Trenker, David A. Agard, Kliment A. Verba, Feng Wang

Publikováno v: Nature, vol 600, iss 7888
Nature

Human epidermal growth factor receptor 2 (HER2) and HER3 form a potent pro-oncogenic heterocomplex1–3 upon binding of growth factor neuregulin-1β (NRG1β). The mechanism by which HER2 and HER3 interact remains unknown in the absence of any structu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc6d4fef99a3ec3123c4687c801715ad
https://doi.org/10.1038/s41586-021-04084-z

Computational pipeline provides mechanistic understanding of Omicron variant of concern neutralizing engineered ACE2 receptor traps

Autor: Soumya G, Remesh, Gregory E, Merz, Axel F, Brilot, Un Seng, Chio, Alexandrea N, Rizo, Thomas H, Pospiech, Irene, Lui, Mathew T, Laurie, Jeff, Glasgow, Chau Q, Le, Yun, Zhang, Devan, Diwanji, Evelyn, Hernandez, Jocelyne, Lopez, Komal Ishwar, Pawar, Sergei, Pourmal, Amber M, Smith, Fengbo, Zhou, Joseph, DeRisi, Tanja, Kortemme, Oren S, Rosenberg, Anum, Glasgow, Kevin K, Leung, James A, Wells, Kliment A, Verba

Publikováno v: bioRxiv

SummaryThe SARS-CoV-2 Omicron variant, with 15 mutations in Spike receptor binding domain (Spike-RBD), renders virtually all clinical monoclonal antibodies against WT SARS-CoV-2 ineffective. We recently engineered the SARS-CoV-2 host entry receptor,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1536ff3a69d8411a0c8b110ffb81d62
https://pubmed.ncbi.nlm.nih.gov/35982665

An effective strategy for ligand-mediated pulldown of the HER2/HER3/NRG1β heterocomplex and cryo-EM structure determination at low sample concentrations

Autor: Raphael Trenker, Devan Diwanji, Kliment A. Verba, Natalia Jura

Publikováno v: Methods Enzymol
Methods in Enzymology ISBN: 9780323915410

Obtaining high-resolution structures of Receptor Tyrosine Kinases that visualize extracellular, transmembrane and intracellular kinase regions simultaneously is an eagerly pursued but still unmet challenge of structural biology. The Human Epidermal G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0788f2ff59424b01525d40e0bec86baf
https://europepmc.org/articles/PMC9288110/

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes

Autor: Jessica K. Peters, Natalia Jura, Aye C. Thwin, Mehdi Bouhaddou, Fei Li, Jocelyne Lopez, Yang Li, Kuei-Ho Chen, Erron W. Titus, Huong T. Kratochvil, Victor L Lam, Christian B. Billesbølle, Tristan W. Owens, Raphael Trenker, Axel F. Brilot, Danielle L. Swaney, Ursula Schulze-Gahmen, Feng Wang, Gregory E. Merz, Jen Chen, Amy Diallo, Yang Zhang, Adam Frost, Soumya G. Remesh, Junrui Li, Edmond Linossi, Fengbo Zhou, Maliheh Safari, Yifan Cheng, Henry C. Nguyen, Andrea Fossati, Devan Diwanji, Evelyn Hernandez, Aashish Manglik, Nevan J. Krogan, Iris D. Young, Jianhua Zhao, Kyle E. Lopez, Alexandrea N. Rizo, Megan Lo, Thomas H. Pospiech, Gwendolyn M. Jang, Y. Li, Sergei Pourmal, Yuan Zhou, Miles Sasha Dickinson, Un Seng Chio, Kaihua Zhang, Caleigh M. Azumaya, Michael D Paul, Oren S. Rosenberg, Yanxin Liu, Tsz Kin Martin Tsui, Carlos Nowotny, Kate Kim, Kliment A. Verba, Loan Doan, Zanlin Yu, Adrian Pelin, Mariano C Tabios, Lorena Zuliani-Alvarez, Daniel R. Southworth, Melody G. Campbell, Ming Sun, Adamo Mancino, Kaitlin Schaefer, Frank R. Moss, Daniel Asarnow, Meghna Gupta, James S. Fraser, Komal Ishwar Pawar, Amber M. Smith, Robert M. Stroud, Tanja Kortemme, Cristina Puchades, Michelle Moritz, Nadia Herrera, Eric Tse, Mingliang Jin, David A. Agard

Publikováno v: bioRxiv
article-version (status) pre
article-version (number) 1
bioRxiv, vol 2, iss 05-19
Research Square

The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f8c3bdd782cfa56f525ccd0d1740780
https://pubmed.ncbi.nlm.nih.gov/34013269