2kes

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{{Seed}}
 
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[[Image:2kes.png|left|200px]]
 
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==Solution Structure of the Coiled-coil Domain of Synphilin-1==
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The line below this paragraph, containing "STRUCTURE_2kes", creates the "Structure Box" on the page.
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<StructureSection load='2kes' size='340' side='right'caption='[[2kes]]' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2kes]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KES FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kes OCA], [https://pdbe.org/2kes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kes RCSB], [https://www.ebi.ac.uk/pdbsum/2kes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kes ProSAT]</span></td></tr>
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{{STRUCTURE_2kes| PDB=2kes | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SNCAP_HUMAN SNCAP_HUMAN] Defects in SNCAIP may be a cause of Parkinson disease (PARK) [MIM:[https://omim.org/entry/168600 168600]. A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.<ref>PMID:11590439</ref> <ref>PMID:12761037</ref> <ref>PMID:18366718</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/SNCAP_HUMAN SNCAP_HUMAN] Isoform 2 inhibits the ubiquitin ligase activity of SIAH1 and inhibits proteasomal degradation of target proteins. Isoform 2 inhibits autoubiquitination and proteasomal degradation of SIAH1, and thereby increases cellular levels of SIAH. Isoform 2 modulates SNCA monoubiquitination by SIAH1.<ref>PMID:16595633</ref> <ref>PMID:19224863</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Solution Structure of the Coiled-coil Domain of Synphilin-1===
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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<ref>PMID:19762560</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2kes" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19762560 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19762560}}
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Parkinson disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603779 603779]]
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==About this Structure==
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2KES is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KES OCA].
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==Reference==
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<ref group="xtra">PMID:19762560</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Hu, H Y.]]
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[[Category: Large Structures]]
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[[Category: Xie, Y Y.]]
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[[Category: Hu HY]]
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[[Category: Zhou, C J.]]
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[[Category: Xie YY]]
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[[Category: Zhou, Z R.]]
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[[Category: Zhou CJ]]
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[[Category: Ank repeat]]
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[[Category: Zhou ZR]]
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[[Category: Coiled-coil]]
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[[Category: Disease mutation]]
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[[Category: Parkinson disease]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Protein binding]]
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[[Category: Synphillin]]
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[[Category: Ubl conjugation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:31:19 2010''
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Current revision

Solution Structure of the Coiled-coil Domain of Synphilin-1

PDB ID 2kes

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