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Conformational Characterization of Synapse-Associated Protein 97 by Nuclear Magnetic Resonance and Small-Angle X-ray Scattering Shows Compact and Elongated Forms

Synapse-associated protein 97 (SAP97) is a membrane-associated guanylate kinase protein that interacts with other proteins such as ion channels, subunits of glutamate receptors, and other cytoskeletal proteins and molecular scaffolds. The molecular diversity of SAP97 results from alternative splicing at the N-terminus, and in the U1 and U5 regions. There are two main N-terminal isoforms: the β-isoform has an L27 domain, whereas in the α-isoform, this is replaced by a palmitoylation motif. We have used multiangle light scattering, nuclear magnetic resonance, and small-angle X-ray scattering studies to characterize the conformation of a truncated form of the β-isoform, hence mimicking the α-isoform. This paper provides a comprehensive view of the small-angle X-ray scattering data, and the resulting data show that the scattering data are consistent with the presence of an ensemble of forms in dynamic equilibrium, with two prominent populations of compact and extended forms, with Rg values of 38 ± 7 Å (52%) a...

Authors:   Mark D. Tully; J. Günter Grossmann; Marie Phelan; Sravan Pandelaneni; Mark Leyland; Lu-Yun Lian
Journal:   Biochemistry
Year:   2012
DOI:   10.1021/bi201178v
Publication date:   19-Jan-2012
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