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

Authors Feng, Wei HKUST affiliated (currently or previously)
Long, Jiafu HKUST affiliated (currently or previously)
Fan, Jingsong HKUST affiliated (currently or previously).
Suetake, Tetsuya HKUST affiliated (currently or previously).
Zhang, Mingjie View this author's profile
Issue Date 2004
Source Nature structural & molecular biology , v. 11, (5), 2004, MAY, p. 475-480
Summary 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 alpha-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.
ISSN 1545-9985
Rights We would like to give credit to Nature Pub. Group for granting us permission to repost this article.
Language English
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