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Article
Nature Structural & Molecular Biology  11, 475 - 480 (2004)
Published online: 28 March 2004; | doi:10.1038/nsmb751

The tetrameric L27 domain complex as an organization platform for supramolecular assemblies

Wei Feng1, 2, Jia-Fu Long1, 2, Jing-Song Fan1, Tetsuya Suetake1 & Mingjie Zhang1

1  Department of Biochemistry, Molecular Neuroscience Center, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.

2  These authors contributed equally to this work.

Correspondence should be addressed to Mingjie Zhang mzhang@ust.hk
L27 domain, initially identified in the Caenorhabditis elegans Lin-2 and Lin-7 proteins, is a protein interaction module that exists in a large family of scaffold proteins. The domain can function as an organization center of large protein assemblies required for establishment and maintenance of cell polarity. We have solved the high-resolution NMR structure of a tetrameric complex of L27 domains containing two SAP97−mLin-2 L27 domain heterodimers. Each L27 domain contains three a-helices. The first two helices of each domain are packed together to form a four-helical bundle in the heterodimer. The third helix of each L27 domain forms another four-helical bundle that assembles the two heterodimers into a tetramer. The structure of the complex provides a mechanistic explanation for L27 domain−mediated polymerization of scaffold proteins, a process that is crucial for the assembly of supramolecular complexes in asymmetric cells.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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