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X‐ray Structures of Binary and Ternary Enzyme‐Product‐Inhibitor Complexes of Matrix Metalloproteinases

2003; Wiley; Volume: 42; Issue: 23 Linguagem: Inglês

10.1002/anie.200350957

1521-3773

Ivano Bertini, V. Calderone, Marco Fragai, Claudio Luchinat, Stefano Mangani, Beatrice Terni,

Peptidase Inhibition and Analysis

Angewandte Chemie International EditionVolume 42, Issue 23 p. 2673-2676 Communication X-ray Structures of Binary and Ternary Enzyme-Product-Inhibitor Complexes of Matrix Metalloproteinases† Ivano Bertini Prof., Ivano Bertini Prof. [email protected] Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorVito Calderone Dr., Vito Calderone Dr. Department of Chemistry, University of Siena, ItalySearch for more papers by this authorMarco Fragai Dr., Marco Fragai Dr. Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorClaudio Luchinat Prof., Claudio Luchinat Prof. Magnetic Resonance Center and, Department of Agricultural Biotechnology, University of Florence, ItalySearch for more papers by this authorStefano Mangani Prof., Stefano Mangani Prof. Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271 Department of Chemistry, University of Siena, ItalySearch for more papers by this authorBeatrice Terni Dr., Beatrice Terni Dr. Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this author Ivano Bertini Prof., Ivano Bertini Prof. [email protected] Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorVito Calderone Dr., Vito Calderone Dr. Department of Chemistry, University of Siena, ItalySearch for more papers by this authorMarco Fragai Dr., Marco Fragai Dr. Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this authorClaudio Luchinat Prof., Claudio Luchinat Prof. Magnetic Resonance Center and, Department of Agricultural Biotechnology, University of Florence, ItalySearch for more papers by this authorStefano Mangani Prof., Stefano Mangani Prof. Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271 Department of Chemistry, University of Siena, ItalySearch for more papers by this authorBeatrice Terni Dr., Beatrice Terni Dr. Magnetic Resonance Center and Department of Chemistry, University of Florence, via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy, Fax: (+39) 055-457-4271Search for more papers by this author First published: 12 June 2003 https://doi.org/10.1002/anie.200350957Citations: 35 † This work was supported by Ente Cassa di Risparmio di Firenze; Fondo per gli investimenti della ricerca di base (MIUR), contract RBNE01TTJW; Fondo integravito speciale per la ricerca (MIUR), “Modeling di strutture di metalloproteine e delle internazioni proteinafarmaco e proteina-proteina. We are grateful to the staff of the ID-14-1- beam line of the European Synchrotron Facility for technical assistance during the X-ray data collection. 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 Graphical Abstract A helicoidal filament results from the approach of the N-terminus of the mutated variant of the catalytic domain of MMP-12 with the catalytic zinc center of another molecule (see X-ray structure); adjacent filaments are arranged in double helices. The N-terminal fragment is proposed to be analogous to an N-terminal polypeptide product after cleavage. Crystals yield two contrasting structures, in which the NH3+ ion is either triply hydrogen bonded, or only exhibits van der Waals interactions. Citing Literature Supporting Information Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2003/z50957_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. Volume42, Issue23June 16, 2003Pages 2673-2676 RelatedInformation