論文

査読有り
2017年12月1日

Conformational landscape mapping the difference between N-lobes and C-lobes of calmodulin

Journal of Inorganic Biochemistry
  • Hiroshi Kawasaki
  • ,
  • Robert H. Kretsinger

177
開始ページ
55
終了ページ
62
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.jinorgbio.2017.08.025
出版者・発行元
Elsevier Inc.

Calmodulin is a calcium binding protein that consists of four EF-hand domains. The two EF-lobes of calmodulin, called the N-lobe and the C-lobe, arose from duplication and fusion of a precursor EF-hand. The amino acid sequences and the structures of the N-lobe and of the C-lobe are quite similar to each other. The N-lobe and the C-lobe, however, have subtle differences in structure and function. We analyzed the helix positions of calmodulin lobes by the alignment with the pseudo-two fold axis of the EF-lobe. We made a map of conformational landscape of helix positions. The four states of the EF-lobe appeared on two lines in the landscape
these two lines show the trajectory of opening and closing of the EF-lobe. For the N-lobe of calmodulin, the calcium bound form and the apo-forms are on the lower line. The two apo-forms of the C-lobe of calmodulin, with target and without target, are on the upper line. The calcium bound form of the C-lobe is on the lower line. The rearrangement of helix interaction between two the EF-hands is necessary for calcium binding in the C-lobe. The hydrophobic packing in the apo-form of the N-lobe is similar to the packing of the N- and C-lobes of the calcium bound form. However, the packing of C-lobe side chains in the apo-form is different from these other three structures. Our detailed analysis should serve as an example that can be applied to other proteins that undergo changes in conformation upon binding effectors.

Web of Science ® 被引用回数 : 6

リンク情報
DOI
https://doi.org/10.1016/j.jinorgbio.2017.08.025
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000419812400006&DestApp=WOS_CPL
URL
http://orcid.org/0000-0002-2517-159X

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