Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/2281

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

Authors Feng, W
Long, JF
Fan, JS
Suetake, T
Zhang, MJ
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.
Subjects
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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