NMR resonance assignments (¹H, ¹³C, ¹⁵N) of jararacin (rJarc), a disintegrin from Bothrops jararaca.

Authors

Jorge Eduardo Chang Estrada, Ariana Azevedo Vasconcelos, Russolina Benedeta Zingali, Fabio C L Almeida

Published in

Biomolecular NMR assignments. Volume 20. Issue 1. Jun 15, 2026. Epub Jun 15, 2026.

Abstract

Disintegrins are a group of cysteine-rich proteins found in a wide variety of snake venoms. These proteins selectively bind to integrins, which play fundamental roles in the regulation of numerous physiological and pathological processes. Here, we report the NMR chemical shift assignments for ¹H, ¹⁵N, and ¹³C nuclei in the backbone and side chains of the recombinant disintegrin jararacin (rJarc). The assignments were further validated by secondary structure prediction using the TALOS-N server. Despite sharing 86.4% sequence identity with jarastatin and 83.6% with trimestatin, rJarc displays a distinct dynamic behavior. Owing to this behavior, the assignment process was challenging due to the lack of observable correlations in triple-resonance experiments for several resonances. Taken together, these data provide an essential basis for NMR-based investigations, including structure determination and characterization of its unique dynamic properties.

PMID:
42295596
Bibliographic data and abstract were imported from PubMed on 15 Jun 2026.

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