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Sci. Signal., 18 September 2012
Vol. 5, Issue 242, p. ec246
[DOI: 10.1126/scisignal.2003609]

EDITORS' CHOICE

Biochemistry Dynamic Assembly

Valda Vinson

Science, AAAS, Washington, DC 20005, USA

Structural characterization of protein complexes has yielded significant insight into biological function; however, most structural techniques require stable, homogeneous samples. This presents a challenge in characterizing transient signaling complexes. Herzog et al. used chemical cross-linking and mass spectroscopy (XL-MS) to characterize the modular and dynamic interaction network involving phosphatase 2A (PP2A), which interacts with tens of regulatory and adaptor proteins in diverse signaling pathways. They found 176 interprotein and 569 intraprotein distance restraints that delineated the topology of the network. The study establishes the importance of XL-MS in the suite of structural methods used to characterize dynamic assemblies.

F. Herzog, A. Kahraman, D. Boehringer, R. Mak, A. Bracher, T. Walzthoeni, A. Leitner, M. Beck, F.-U. Hartl, N. Ban, L. Malmström, R. Aebersold, Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry. Science 337, 1348–1352 (2012). [Abstract] [Full Text]

Citation: V. Vinson, Dynamic Assembly. Sci. Signal. 5, ec246 (2012).


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