TAILIEUCHUNG - Báo cáo khoa học: What determines the degree of compactness of a calcium-binding protein?

The EF-hand calcium-binding proteins may exist either in an extended or a compact conformation. This conformation is sometimes correlated with the function of the calcium-binding protein. For those proteins whose structure and function are known, calcium sensors are usually extended and calcium buffers compact; hence, there is interest in predicting the form of the pro-tein starting from its sequence. | ễFEBS Journal What determines the degree of compactness of a calcium-binding protein Liliane Mouawad1 Adriana Isvoran2 Eric Quiniou1 and Constantin T. Craescu1 1 Inserm U759 Institut Curie-Recherche Centre Universitaire Paris-Sud Orsay France 2 Department of Chemistry West University of Timisoara Romania Keywords calcium-binding proteins centrin EF-hand hydrophobicity predicted form Correspondence L. Mouawad Inserm U759 Institut Curie-Recherche Centre Universitaire Paris-Sud Bailment 112 91405 Orsay Cedex France Fax 33 1 69 07 53 27 Tel 33 1 69 86 71 51 E-mail Received 8 September 2008 revised 8 December 2008 accepted 10 December 2008 doi The EF-hand calcium-binding proteins may exist either in an extended or a compact conformation. This conformation is sometimes correlated with the function of the calcium-binding protein. For those proteins whose structure and function are known calcium sensors are usually extended and calcium buffers compact hence there is interest in predicting the form of the protein starting from its sequence. In the present study we used two different procedures one that already exists in the literature the SOSUIDUMBBELL algorithm mainly based on the charges of the two EF-hand domains and the other comprising a novel procedure that is based on linker average hydrophilicity. The linker consists of the residues that connect the domains. The two procedures were tested on 17 known-structure calcium-binding proteins and then applied to 59 unknown-structure centrins. The SOSUI-DUMBBELL algorithm yielded the correct conformations for only 15 of the known-structure proteins and predicted that all centrins should be in a closed form. The linker average hydrophilicity procedure discriminated well between all the extended and non-extended forms of the known-structure calcium-binding proteins and its prediction concerning centrins reflected well their phylogenetic classification. The linker

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