Calcium Binding Dramatically Stabilizes an Ancestral Crystallin Fold in Tunicate βγ-Crystallin
Author:
Affiliation:
1. Department of Chemistry, University of California, Irvine, California 92697-2025, United States
2. Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, United States
Funder
National Eye Institute
Division of Materials Research
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00937
Reference27 articles.
1. NMR Assignment of M-crystallin: A Novel Ca2+ Binding Protein of the βγ-crystallin Superfamily from Methanosarcina acetivorans
2. Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens βγ-crystallins
3. Urochordate βγ-Crystallin and the Evolutionary Origin of the Vertebrate Eye Lens
4. Evolutionary relationships of the metazoan βγ–crystallins, including that from the marine spongeGeodia cydonium
5. Disability for Function: Loss of Ca2+-Binding Is Obligatory for Fitness of Mammalian βγ-Crystallins
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3. Replica exchange molecular dynamics simulations reveal self-association sites in M-crystallin caused by mutations provide insights of cataract;Scientific Reports;2021-12
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