Reading List

Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli

1. Ralf Steinhilper
2. Gabriele Höff
3. Johann Heider
4. Bonnie J. Murphy

Solvent-induced allosteric transition of the Hepatitis C virus human cellular receptor CD81 large extracellular loop

1. C. Risueño
2. D. Charro
3. N. G. A. Abrescia
4. I. Coluzza

Computational study of ion permeation through claudin‐4 paracellular channels

1. Alessandro Berselli
2. Giulio Alberini
3. Fabio Benfenati
4. Luca Maragliano

Human myelin proteolipid protein structure and lipid bilayer stacking

1. Salla Ruskamo
2. Arne Raasakka
3. Jan Skov Pedersen
4. Anne Martel
5. Karel Škubník
6. Tamim Darwish
7. Lionel Porcar
8. Petri Kursula

Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery

1. Vidya Mangala Prasad
2. Jelle S. Blijleven
3. Jolanda M. Smit
4. Kelly K. Lee

Ion channel model reduction using manifold boundaries

1. Dominic G. Whittaker
2. Jiahui Wang
3. Joseph G. Shuttleworth
4. Ravichandra Venkateshappa
5. Jacob M. Kemp
6. Thomas W. Claydon
7. Gary R. Mirams

mPPases create a conserved anionic membrane fingerprint as identified via multi-scale simulations

1. Alexandra O. M. Holmes
2. Adrian Goldman
3. Antreas C. Kalli

Excitatory and inhibitory D-serine binding to the NMDA receptor

1. Remy A Yovanno
2. Tsung Han Chou
3. Sarah J Brantley
4. Hiro Furukawa
5. Albert Y Lau

• Curated by eLife

  Evaluation Summary:

  Activation of NMDA receptors requires two co-agonists: Glutamate which binds to the GluN2 subunit and glycine/D-serine which binds to the GluN1 subunit. In the present manuscript, the authors address the interaction of D-serine, which is a less studied co-agonist than glycine, with the GluN1 and GluN2A subunits using molecular simulations as well as electrophysiology experiments. Surprisingly they find that D-serine interacts with the GluN2 subunit, further expanding our molecular understanding of NMDA receptor structure-function.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 and Reviewer #2 agreed to share their names with the authors.)

Reviewed by eLife

High Calcium Transport by Polycystin-2 (TRPP2) Induces Channel Clustering and Coordinated Oscillatory Behavior

1. Irina F. Velázquez
2. Horacio F. Cantiello
3. María del Rocío Cantero

Proton-driven alternating access in a spinster transporter, an emerging family of broad-specificity efflux pumps

1. Reza Dastvan
2. Ali Rasouli
3. Sepehr Dehghani-Ghahnaviyeh
4. Samantha Gies
5. Emad Tajkhorshid

Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport

1. Jiemin Shen
2. Miaohui Hu
3. Xiao Fan
4. Zhenning Ren
5. Corinne Portioli
6. Xiuwen Yan
7. Mingqiang Rong
8. Ming Zhou

Cryo‐EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms

1. Le Thi My Le
2. James Robert Thompson
3. Sepehr Dehghani‐Ghahnaviyeh
4. Shashank Pant
5. Phuoc Xuan Dang
6. Jarrod Bradley French
7. Takahisa Kanikeyo
8. Emad Tajkhorshid
9. Amer Alam

Fly-casting with ligand–sliding and orientational selection to support the complex formation of a GPCR and a middle-sized flexible molecule

1. Junichi Higo
2. Kota Kasahara
3. Gert-Jan Bekker
4. Benson Ma
5. Shun Sakuraba
6. Shinji Iida
7. Narutoshi Kamiya
8. Ikuo Fukuda
9. Hidetoshi Kono
10. Yoshifumi Fukunishi
11. Haruki Nakamura

Ligand-mediated Structural Dynamics of a Mammalian Pancreatic KATP Channel

1. Min Woo Sung
2. Camden M. Driggers
3. Barmak Mostofian
4. John D. Russo
5. Bruce L. Patton
6. Daniel M. Zuckerman
7. Show-Ling Shyng

Structural motifs for subtype-specific pH-sensitive gating of vertebrate otopetrin proton channels

1. Bochuan Teng
2. Joshua P Kaplan
3. Ziyu Liang
4. Zachary Krieger
5. Yu-Hsiang Tu
6. Batuujin Burendei
7. Andrew B Ward
8. Emily R Liman

• Curated by eLife

  Evaluation Summary:

  The manuscript shows that OTOP proton channels are proton-gated with distinct pH sensitivities, and identifies regions on the proteins that alter pH-dependent gating. The main claims are well supported by the data. These findings are likely to be of interest to researchers studying acid/base physiology, sensory physiology, or ion channel biophysics.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 and Reviewer #3 agreed to share their name with the authors.)

Reviewed by eLife

Transition between conformational states of the TREK-1 K2P channel promoted by interaction with PIP2

1. Adisorn Panasawatwong
2. Tanadet Pipatpolkai
3. Stephen J. Tucker

Cryo-EM structure of the Rhodobaca bogoriensis RC-LH1-PufX dimeric complex at 2.9 Å

1. Dmitry A. Semchonok
2. Marina I. Siponen
3. Christian Tüting
4. Quentin Charras
5. Fotis L. Kyrilis
6. Farzad Hamdi
7. Yashar Sadian
8. Colette Jungas
9. Panagiotis L. Kastritis

Structural basis for receptor selectivity and inverse agonism in S1P5 receptors

1. Elizaveta Lyapina
2. Egor Marin
3. Anastasiia Gusach
4. Philipp Orekhov
5. Andrey Gerasimov
6. Aleksandra Luginina
7. Daniil Vakhrameev
8. Margarita Ergasheva
9. Margarita Kovaleva
10. Georgii Khusainov
11. Polina Khorn
12. Mikhail Shevtsov
13. Kirill Kovalev
14. Sergey Bukhdruker
15. Ivan Okhrimenko
16. Petr Popov
17. Hao Hu
18. Uwe Weierstall
19. Wei Liu
20. Yunje Cho
21. Ivan Gushchin
22. Andrey Rogachev
23. Gleb Bourenkov
24. Sehan Park
25. Gisu Park
26. Hyo Jung Hyun
27. Jaehyun Park
28. Valentin Gordeliy
29. Valentin Borshchevskiy
30. Alexey Mishin
31. Vadim Cherezov

Structural and temporal basis for agonism in the α4β2 nicotinic acetylcholine receptor

1. A. Sofia F. Oliveira
2. Isabel Bermudez
3. Timothy Gallagher
4. Susan Wonnacott
5. Giovanni Ciccotti
6. Richard B. Sessions
7. Adrian J. Mulholland

Structural insights into the peptide selectivity and activation of human neuromedin U receptors

1. Chongzhao You
2. Yumu Zhang
3. Peiyu Xu
4. Sijie Huang
5. Wanchao Yin
6. H. Eric Xu
7. Yi Jiang