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- Title
The tetrameric L27 domain complex as an organization platform for supramolecular assemblies.
- Authors
Wei Feng; Jie-Fu Long; Jing-Song Fan; Suetake, Tetsuya; Mingjie Zhang
- Abstract
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 _-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.
- Subjects
CAENORHABDITIS elegans; PROTEINS; SUPRAMOLECULAR chemistry; POLYMERS; POLYMERIZATION; ASYMMETRIC synthesis; CELLS
- Publication
Nature Structural & Molecular Biology, 2004, Vol 11, Issue 5, p475
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb751