HKUST Library Institutional Repository Banner

HKUST Institutional Repository >
Biochemistry >
BICH Journal/Magazine Articles >

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

Files in This Item:

File Description SizeFormat
nsmb751_L27.pdf811KbAdobe PDFView/Open

Find published version via OpenURL Link Resolver

All items in this Repository are protected by copyright, with all rights reserved.