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  Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation.

Behrens, C., Binotti, B., Schmidt, C., Robinson, C. V., Chua, J. J. E., & Kühnel, K. (2013). Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation. PLoS One, 8(10): e76355. doi:10.1371/journal.pone.0076355.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-9AC7-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CEEA-6
Genre: Journal Article

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Behrens, C.1, Author              
Binotti, B.1, Author              
Schmidt, C., Author
Robinson, C. V., Author
Chua, J. J. E.2, Author              
Kühnel, K.1, Author              
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              
2Research Group of Protein Trafficking in Synaptic Development and Function, MPI for Biophysical Chemistry, Max Planck Society, ou_1933287              

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 Abstract: The short coiled coil protein (SCOC) forms a complex with fasciculation and elongation protein zeta 1 (FEZ1). This complex is involved in autophagy regulation. We determined the crystal structure of the coiled coil domain of human SCOC at 2.7 angstrom resolution. SCOC forms a parallel left handed coiled coil dimer. We observed two distinct dimers in the crystal structure, which shows that SCOC is conformationally flexible. This plasticity is due to the high incidence of polar and charged residues at the core a/d-heptad positions. We prepared two double mutants, where these core residues were mutated to either leucines or valines (E93V/K97L and N125L/N132V). These mutations led to a dramatic increase in stability and change of oligomerisation state. The oligomerisation state of the mutants was characterized by multi-angle laser light scattering and native mass spectrometry measurements. The E93V/K97 mutant forms a trimer and the N125L/N132V mutant is a tetramer. We further demonstrate that SCOC forms a stable homogeneous complex with the coiled coil domain of FEZ1. SCOC dimerization and the SCOC surface residue R117 are important for this interaction.

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Language(s): eng - English
 Dates: 2013-10-01
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1371/journal.pone.0076355
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Title: PLoS One
Source Genre: Journal
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Pages: 12 Volume / Issue: 8 (10) Sequence Number: e76355 Start / End Page: - Identifier: -