Academic Journal

Comparison of the structure-function of five newly members of the calcin family

التفاصيل البيبلوغرافية
العنوان: Comparison of the structure-function of five newly members of the calcin family
المؤلفون: Hua X., Yao J., Liu X., Liu Q., Deng Y., Li S., Valdivia C. R., Wang F., Pozzolini M., Shou Z., Valdivia H. H., Xiao L.
المساهمون: Hua, X., Yao, J., Liu, X., Liu, Q., Deng, Y., Li, S., Valdivia, C. R., Wang, F., Pozzolini, M., Shou, Z., Valdivia, H. H., Xiao, L.
بيانات النشر: ELSEVIER
RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
سنة النشر: 2024
المجموعة: Università degli Studi di Genova: CINECA IRIS
مصطلحات موضوعية: Calcin, Dynamic simuation, Molecular docking, Ryanodine receptor, [(3)H]ryanodine binding
الوصف: Calcins are a group of scorpion toxin peptides specifically binding to ryanodine receptors (RyRs) with high affinity, and have the ability to activate and stabilize RyR in a long-lasting subconductance state. Five newly calcins synthesized compounds exhibit typical structural characteristics of a specific family through chemical synthesis and virtual analysis. As the calcins from the same species, Petersiicalcin1 and Petersiicalcin2, Jendekicalcin2 and Jendekicalcin3, have only one residue difference. Both Petersiicalcin1 and Petersiicalcin2 exhibited different affinities in stimulating [3H]ryanodine binding, but the residue mutation resulted in a 2.7 folds difference. Other calcins also exhibited a stimulatory effect on [3H]ryanodine binding to RyR1, however, their affinities were significantly lower than that of Petersiiicalcin1 and Petersiiicalcin2. The channel domain of RyR1 was found to be capable of binding with the basic residues of these calcins, which also exhibited interactions with the S6 helices on RyR1. Dynamic simulations were conducted for Petersiicalcin1 and Petersiicalcin2, which demonstrated their ability to form a highly stable conformation and resulting in an asymmetric tetramer structure of RyR1. The discovery of five newly calcins further enriches the diversity of the natural calcin family, which provides more native peptides for the structure-function analysis between calcin and RyRs.
نوع الوثيقة: article in journal/newspaper
وصف الملف: ELETTRONICO
اللغة: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/38219929; info:eu-repo/semantics/altIdentifier/wos/WOS:001161301300001; volume:260; issue:Pt 1; firstpage:1; lastpage:11; numberofpages:11; journal:INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES; https://hdl.handle.net/11567/1179957; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85182738024
DOI: 10.1016/j.ijbiomac.2024.129424
الاتاحة: https://hdl.handle.net/11567/1179957
https://doi.org/10.1016/j.ijbiomac.2024.129424
رقم الانضمام: edsbas.1CDE62D7
قاعدة البيانات: BASE
الوصف
DOI:10.1016/j.ijbiomac.2024.129424