1RSO

Hetero-tetrameric L27 (Lin-2, Lin-7) domain complexes as organization platforms of supra-molecular assemblies

Summary for 1RSO

• Entry DOI: 10.2210/pdb1rso/pdb
• Descriptor: Presynaptic protein SAP97, Peripheral plasma membrane protein CASK (2 entities in total)
• Functional Keywords: l27 domain, scaffold protein, protein assembly, cell polarity, neuropeptide-membrane protein complex, neuropeptide/membrane protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Membrane; Peripheral membrane protein (By similarity): Q62696; Nucleus: Q62915
• Total number of polymer chains: 4
• Total formula weight: 27130.19

Authors

Feng, W.,Long, J.-F.,Fan, J.-S.,Suetake, T.,Zhang, M. (deposition date: 2003-12-09, release date: 2004-05-04, Last modification date: 2024-05-29)

Primary citation

Feng, W.,Long, J.-F.,Fan, J.-S.,Suetake, T.,Zhang, M.
The tetrameric L27 domain complex as an organization platform for supramolecular assemblies
NAT.STRUCT.MOL.BIOL., 11:475-480, 2004

PubMed 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 a-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.

PubMed: 15048107
DOI: 10.1038/nsmb751

Experimental method

SOLUTION NMR