Nature Search

Cryo-EM structures of NHEJ assemblies with nucleosomes

DNA double-strand breaks endanger genome stability. Here, the authors present cryo-EM structures showing how Ku70/80 and DNA-PK bind DNA ends on nucleosomes, offering a mechanistic model for break recognition within chromatin.

Chloe Hall
Philippe Frit
Amanda K. Chaplin
ResearchOpen Access24 Dec 2025
Nature Communications

Volume: 17, P: 1-13
Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding

Dimitri Y. Chirgadze
Jonathan P. Hepple
Ermanno Gherardi
Research01 Jan 1999
Nature Structural Biology

Volume: 6, P: 72-79
Publisher Correction: Mechanisms of inhibition and activation of extrasynaptic αβ GABA_A receptors

Vikram Babu Kasaragod
Martin Mortensen
Paul S. Miller
Amendments and CorrectionsOpen Access24 Mar 2022
Nature

Volume: 604, P: E15
Nanostructured films from hierarchical self-assembly of amyloidogenic proteins

Well-ordered and highly rigid macroscopic films can be self-assembled from amyloid protein fibrils.

Tuomas P. J. Knowles
Tomas W. Oppenheim
Mark E. Welland
Research28 Feb 2010
Nature Nanotechnology

Volume: 5, P: 204-207
Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats

If broken chromosomes arising from DNA double-strand breaks are left unrepaired or incorrectly repaired, they can lead to genomic changes that may result in cell death or cancer. DNA-dependent protein kinase (DNA-PK), which comprises the DNA-PK catalytic subunit (DNA-PKcs) and the heterodimer Ku70/Ku80, has a major role in the repair of double-strand breaks. The crystal structure of human DNA-PKcs is now presented, in which the overall fold is clearly visible.

Bancinyane L. Sibanda
Dimitri Y. Chirgadze
Tom L. Blundell
Research20 Dec 2009
Nature

Volume: 463, P: 118-121
The molecular basis of drug selectivity for α5 subunit-containing GABA_A receptors

Here, Kasaragod et al. solve structures of the GABA_A receptor α5 subunit in complex with different classes of positive and negative allosteric modulators to explain the binding modes and the molecular basis of selectivity.

Vikram Babu Kasaragod
Tomas Malinauskas
Paul S. Miller
ResearchOpen Access30 Oct 2023
Nature Structural & Molecular Biology

Volume: 30, P: 1936-1946
Dimers of DNA-PK create a stage for DNA double-strand break repair

A new cryo-EM structure of human DNA-PKcs in complex with a Ku70/80 heterodimer and DNA reveals how Ku80–DNA-PKcs interactions create a scaffold to mediate DNA double-strand break repair.

Amanda K. Chaplin
Steven W. Hardwick
Tom L. Blundell
Research19 Oct 2020
Nature Structural & Molecular Biology

Volume: 28, P: 13-19
Mechanisms of inhibition and activation of extrasynaptic αβ GABA_A receptors

Cryo-electron microscopy structures are used to identify mechanisms underlying distinct features of extrasynaptic type A γ-aminobutyric acid receptors.

Vikram Babu Kasaragod
Martin Mortensen
Paul S. Miller
ResearchOpen Access09 Feb 2022
Nature

Volume: 602, P: 529-533
Single-particle cryo-EM at atomic resolution

Advances in electron cryo-microscopy hardware allow proteins to be studied at atomic resolution.

Takanori Nakane
Abhay Kotecha
Sjors H. W. Scheres
Research21 Oct 2020
Nature

Volume: 587, P: 152-156
Structure and dynamics of Toll immunoreceptor activation in the mosquito Aedes aegypti

Aedes aegypti can act as a vector for viral pathogens but the mechanism of viral resistance and evolving host-pathogen tolerance are poorly understood. Here the authors structurally characterise a duplicated pair of interacting Toll immunoreceptors and the cytokine ligand Spaetzle1C and show their dose-dependent function and mechanism of activation.

Yoann Saucereau
Thomas H. Wilson
Monique Gangloff
ResearchOpen Access30 Aug 2022
Nature Communications

Volume: 13, P: 1-14
Structural basis for human mitochondrial tRNA maturation

Mitochondrial tRNAs are less structurally stable than nuclear tRNAs, and their maturation pathway is unique. Here, the authors reveal how human mitochondrial precursor tRNAs are recognised, processed, methylated and prepared for full functionality in mitochondrial translation.

Vincent Meynier
Steven W. Hardwick
Carine Tisné
ResearchOpen Access01 Jun 2024
Nature Communications

Volume: 15, P: 1-16
5-Formylcytosine alters the structure of the DNA double helix

5-Formylcytosine (5fC) is implicated in active DNA demethylation and has been proposed to act as an epigenetic signal. Balasubramanian and colleagues now report that this base modification imparts a unique, previously undescribed conformation to DNA.

Eun-Ang Raiber
Pierre Murat
Shankar Balasubramanian
Research15 Dec 2014
Nature Structural & Molecular Biology

Volume: 22, P: 44-49
Differential assembly diversifies GABA_A receptor structures and signalling

The diverse makeup and assembly of subunits augment the structure, physiology and pharmacology of GABA_A receptors.

Andrija Sente
Rooma Desai
A. Radu Aricescu
Research30 Mar 2022
Nature

Volume: 604, P: 190-194
Zn(II) mediates vancomycin polymerization and potentiates its antibiotic activity against resistant bacteria

Ashraf Zarkan
Heather-Rose Macklyne
Hee-Jeon Hong
ResearchOpen Access07 Jul 2017
Scientific Reports

Volume: 7, P: 1-9
Structural insights into inhibitor regulation of the DNA repair protein DNA-PKcs

Cryo-electron microscopy structures of DNA-dependent protein kinase catalytic subunit bound to ATPγS and four inhibitors (wortmannin, NU7441, AZD7648 and M3814) provide molecular details and insights useful for drug design.

Shikang Liang
Sherine E. Thomas
Tom L. Blundell
ResearchOpen Access05 Jan 2022
Nature

Volume: 601, P: 643-648
Characterization and structural determination of a new anti-MET function-blocking antibody with binding epitope distinct from the ligand binding domain

Danielle M. DiCara
Dimitri Y. Chirgadze
John McCafferty
ResearchOpen Access21 Aug 2017
Scientific Reports

Volume: 7, P: 1-13

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