Structural Plasticity and Functional Dynamics of Pigeon Cryptochrome 4 as Avian Magnetoreceptor.

ABSTRACT: Cryptochromes (CRYs) are key flavoproteins involved in biological processes such as circadian rhythm regulation and magnetoreception. Type IV CRYs have been identified as primary candidates for avian magnetoreception. However, their structural flexibility, particularly within the cryptochrome C-terminal extension (CCE) and phosphate-binding loop (PBL), remains poorly understood. In this study, we employed temperature replica exchange molecular dynamics (T-REMD) simulations combined with advanced dimensionality reduction techniques, including autoencoder and time-lagged independent component analysis (t-ICA), to explore the conformational space of Columba livia cryptochrome 4 (ClCRY4), as the only available crystal structure of Type IV CRYs to date. By using Drosophila cryptochrome (dCRY) a

SUBMITTER: Xiong C 

PROVIDER: S-EPMC12276989 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature