issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

September 2026 issue

Highlighted illustration

Cover illustration: The crystal structure of the NKX2-1 homeodomain bound to a 19 bp DNA duplex containing two palindromically arranged NK2-recognition motifs [Mohandas & Nam (2026), Acta Cryst. F82, 295–300]. NKX2-1 (thyroid transcription factor 1, TTF-1) is a homeodomain transcription factor that plays critical roles in the development and function of the thyroid, lung and forebrain. The structure provides a structural basis for sequence-specific DNA recognition by NKX2-1 and a framework for interpreting the effects of disease-associated variants.

research communications


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Crystal structures of rice L-galactose dehydrogenase in apo and NAD+-bound forms reveal a conserved architecture and flexible loop regions that are involved in cofactor and substrate binding.

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The crystal structure of the NKX2-1 homeodomain bound to DNA reveals the arrangement of two homeodomains on a palindromic NK2-recognition sequence and provides insight into disease-associated variants.

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Structural and binding studies of the engineered lipocalin CL31d towards the chelate complexes of 11 different lanthanide and main-group metal(III) ions, whose radioisotopes are useful for nuclear medicine, with a functionalized DTPA revealed a surprisingly broad tolerance towards varying ionic radii, thus enabling flexible radionuclide-targeting strategies.

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We present the ZER1–NLRP1 Gly/N-degron structure, revealing a conserved binding cavity for N-terminal glycine recognition. ZER1 binds more weakly than ZYG11B due to distinct interactions at position 3, providing mechanistic insights into NLRP1 inflammasome regulation.

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The crystal structure of peptidyl-tRNA hydrolase 2 from Candidatus Lokiarchaeum sp. GC14_75 (LokiPth2) shows conformational rearrangements that may be associated with substrate recognition and catalysis. In addition, analysis of the optimal temperature for LokiPth2 activity suggests that this archaeon is a moderate thermophile.