Crystal structure of the dynamin tetramer

Thomas F. Reubold, Katja Faelber (), Nuria Plattner, York Posor, Katharina Ketel, Ute Curth, Jeanette Schlegel, Roopsee Anand, Dietmar J. Manstein, Frank Noé, Volker Haucke, Oliver Daumke () and Susanne Eschenburg ()
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Thomas F. Reubold: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover
Katja Faelber: Max-Delbrück-Centrum für Molekulare Medizin, Kristallographie
Nuria Plattner: Institut für Mathematik, Freie Universität Berlin
York Posor: Leibniz-Institut für Molekulare Pharmakologie
Katharina Ketel: Leibniz-Institut für Molekulare Pharmakologie
Ute Curth: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover
Jeanette Schlegel: Max-Delbrück-Centrum für Molekulare Medizin, Kristallographie
Roopsee Anand: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover
Dietmar J. Manstein: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover
Frank Noé: Institut für Mathematik, Freie Universität Berlin
Volker Haucke: Leibniz-Institut für Molekulare Pharmakologie
Oliver Daumke: Max-Delbrück-Centrum für Molekulare Medizin, Kristallographie
Susanne Eschenburg: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover

Nature, 2015, vol. 525, issue 7569, 404-408

Abstract: The crystal structure of the large GTPase dynamin tetramer is presented, suggesting a mechanism by which oligomerization of dynamin is regulated, and revealing how mutations that interfere with tetramer formation and autoinhibition are of relevance to understanding the congenital muscle disorders Charcot–Marie–Tooth neuropathy and centronuclear myopathy.

Date: 2015
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DOI: 10.1038/nature14880

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