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Structural Interplay between Calcium( II ) and Copper( II ) Binding to S100A13 Protein

2005; Wiley; Volume: 44; Issue: 39 Linguagem: Inglês

10.1002/anie.200500540

1521-3773

Fabio Arnesano, Lucia Banci, Ivano Bertini, Adele Fantoni, Leonardo Tenori, Maria Silvia Viezzoli,

Venomous Animal Envenomation and Studies

Angewandte Chemie International EditionVolume 44, Issue 39 p. 6341-6344 Communication Structural Interplay between Calcium(II) and Copper(II) Binding to S100A13 Protein† Fabio Arnesano Dr., Fabio Arnesano Dr. Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorLucia Banci Prof., Lucia Banci Prof. Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorIvano Bertini Prof., Ivano Bertini Prof. [email protected] Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorAdele Fantoni, Adele Fantoni Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorLeonardo Tenori, Leonardo Tenori Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorMaria Silvia Viezzoli Prof., Maria Silvia Viezzoli Prof. Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this author Fabio Arnesano Dr., Fabio Arnesano Dr. Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorLucia Banci Prof., Lucia Banci Prof. Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorIvano Bertini Prof., Ivano Bertini Prof. [email protected] Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorAdele Fantoni, Adele Fantoni Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorLeonardo Tenori, Leonardo Tenori Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorMaria Silvia Viezzoli Prof., Maria Silvia Viezzoli Prof. Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this author First published: 30 September 2005 https://doi.org/10.1002/anie.200500540Citations: 31 † This work was supported by the European Commission (SPINE contract QLG2-CT-2002-00988). The Italian MURST COFIN03 is acknowledged for financial support. Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Graphical Abstract New binding sites: Calcium(II) binding to the dimeric protein S100A13 triggers key conformational changes, thus creating two symmetrical copper(II)-binding sites between the helices of the monomers (see picture). These solvent-exposed binding sites are unique among the S100 proteins. Citing Literature Supporting Information Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2005/z500540_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article. Volume44, Issue39October 7, 2005Pages 6341-6344 RelatedInformation