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2jn5
From Proteopedia
| 2jn5, 10 NMR models () | |||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||
| Coordinates: | save as pdb, mmCIF, xml | ||||
Solution Structure of a Dodecapeptide from Alpha-Synuclein Bound with Synphilin-1
alpha-Synuclein (alpha-Syn) is the major component of Lewy bodies (LBs) deposited in the brains of patients with Parkinson's disease. Synphilin-1 (Sph1) is a novel alpha-Syn-interacting protein also present in the LBs. However, the roles of alpha-Syn-Sph1 interaction in LB formation and in the related pathogenesis are still unclear. We have studied the interaction between alpha-Syn and Sph1 by biochemical and structural approaches and found that the central coiled-coil domain of Sph1 specifically interacts with the N-terminal stretch of alpha-Syn. When overexpressed in HEK 293T cells, Sph1 forms inclusions together with alpha-Syn, but the Sph1-positive inclusions cannot recruit the N-terminally truncated alpha-Syn. The central portion of Sph1 can also recruit alpha-Syn and induce inclusion formation through its coiled-coil domain. These observations demonstrate that the alpha-Syn-Sph1 interaction significantly promotes the formation of cytoplasmic alpha-Syn inclusions, which may have implications for LB formation in neural cells. We have also elucidated solution structure of the coiled-coil domain of Sph1 and its interaction with the N-terminal peptide of alpha-Syn. The specific interaction between alpha-Syn and Sph1 provides mechanistic insights into the inclusion-body formation in cells and pathological implication in Parkinson's disease.
Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication., Xie YY, Zhou CJ, Zhou ZR, Hong J, Che MX, Fu QS, Song AX, Lin DH, Hu HY, FASEB J. 2010 Jan;24(1):196-205. Epub 2009 Sep 17. PMID:19762560
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2JN5 is a 1 chain structure. Full experimental information is available from OCA.
Reference
- Xie YY, Zhou CJ, Zhou ZR, Hong J, Che MX, Fu QS, Song AX, Lin DH, Hu HY. Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication. FASEB J. 2010 Jan;24(1):196-205. Epub 2009 Sep 17. PMID:19762560 doi:fj.09-133082
Page seeded by OCA on Wed May 12 10:35:04 2010
