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http://hdl.handle.net/1783.1/2281
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| Title: | The tetrameric L27 domain complex as an organization platform for supramolecular assemblies |
| Authors: | Feng, Wei
Long, Jiafu
Fan, Jing-Song
Suetake, Tetsuya
Zhang, Mingjie |
| Keywords: | L27 domain
Protein interaction module
Organization platform
Supramolecular assemblies
Scaffold proteins |
| Issue Date: | May-2004 |
| Citation: | Nature structural & molecular biology, vol. 11, no. 5, May 2004, p. 475-480 |
| 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 α-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. |
| Rights: | We would like to give credit to Nature Pub. Group for granting us permission to repost this article. |
| URI: | http://hdl.handle.net/1783.1/2281 |
| Appears in Collections: | BICH Journal/Magazine Articles
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| nsmb751_L27.pdf | | 811Kb | Adobe PDF | View/Open |
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