Structural highlights
3q29 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Related: | 3q25, 3q26, 3q27, 3q28 |
| Gene: | SNCA (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
Publication Abstract from PubMed
Aggregates of the protein alpha-synuclein are the main component of Lewy bodies, the hallmark of Parkinson's disease. alpha-Synuclein aggregates are also found in many human neurodegenerative diseases known as synucleinopathies. In vivo, alpha-synuclein associates with membranes and adopts alpha-helical conformations. The details of how alpha-synuclein converts from the functional native state to amyloid aggregates remain unknown. In this study, we use maltose-binding protein (MBP) as a carrier to crystallize segments of alpha-synuclein. From crystal structures of fusions between MBP and four segments of alpha-synuclein, we have been able to trace a virtual model of the first 72 residues of alpha-synuclein. Instead of a mostly alpha-helical conformation observed in the lipid environment, our crystal structures show alpha-helices only at residues 1-13 and 20-34. The remaining segments are extended loops or coils. All of the predicted fiber-forming segments based on the 3D profile method are in extended conformations. We further show that the MBP fusion proteins with fiber-forming segments from alpha-synuclein can also form fiber-like nano-crystals or amyloid-like fibrils. Our structures suggest intermediate states during amyloid formation of alpha-synuclein.
Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation.,Zhao M, Cascio D, Sawaya MR, Eisenberg D Protein Sci. 2011 Jun;20(6):996-1004. doi: 10.1002/pro.630. Epub 2011 May, 3. PMID:21462277[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao M, Cascio D, Sawaya MR, Eisenberg D. Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation. Protein Sci. 2011 Jun;20(6):996-1004. doi: 10.1002/pro.630. Epub 2011 May, 3. PMID:21462277 doi:10.1002/pro.630
