Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasite Plasmodium falciparum

Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasite Plasmodium falciparum

Abstract Calmodulin (CaM), the key calcium sensor of eukaryotic cells regulating a great number of target proteins, belongs to the most conserved proteins. We compared function and properties of CaMs from two evolutionarily distant species, the human (Homo sapiens) representing vertebrates, and the...

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Bibliographic Details
Main Authors: Tünde Juhász, József Kardos, Zsolt Dürvanger, Veronika Harmat, Károly Liliom
Format: Article
Language:English
Published: Wiley 2020-08-01
Series:FASEB BioAdvances
Subjects:
binding affinity
inhibitor development
protein stability
protein structure
target activation
Online Access:https://doi.org/10.1096/fba.2020-00013

Internet

https://doi.org/10.1096/fba.2020-00013

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