issue contents

ISSN: 2053-230X

March 2021 issue

Highlighted illustration

Cover illustration: Human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP [Shaikhqasem et al. (2021), Acta Cryst. F77, 70-78]. CRM1 is a nuclear export receptor that has been important in the development of antitumor and antiviral drugs. Structural analysis of several inhibitor compounds bound to CRM1 revealed that their mechanism of action relies on the covalent modification of a critical cysteine residue (Cys528 in the human receptor) located in the nuclear export signal-binding cleft.

research communications

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Structural comparison of the apo form of Saccharomyces cerevisiae anthranilate phosphoribosyltransferase with structures of its complexes with PRPP or the substrate analogue 4-fluoroanthranilate provide structural insights into substrate binding.

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The covalent modification of human CRM1 by 2-mercaptoethanol interferes with the characterization of cysteine-dependent inhibitor compounds.

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The isolated complex of the TF55β chaperonin from the thermophilic archaeon Sulfolobus solfataricus are reported. The structures of nucleotide-bound complexes of TF55β obtained at 3.6–4.2 Å resolution using cryo-EM reveal an open conformation.

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Cadherin-17, a 7D-cadherin, has N-terminal extracellular cadherin (EC) repeats similar to those of classical cadherins but with several key differences that are relevant to its biological function. The structure presented here demonstrates that cadherin-17 is incapable of forming the EC1 tryptophan-mediated strand-swap conformation that classical cadherins use to adhere cells together.
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