2n04
From Proteopedia
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==Solution Structure of the phosphorylated N-terminal region of Human Cysteine String Protein (CSP)== | ==Solution Structure of the phosphorylated N-terminal region of Human Cysteine String Protein (CSP)== | ||
| - | <StructureSection load='2n04' size='340' side='right' caption='[[2n04 | + | <StructureSection load='2n04' size='340' side='right'caption='[[2n04]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2n04]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N04 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[2n04]] 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=2N04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N04 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n04 OCA], [https://pdbe.org/2n04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n04 RCSB], [https://www.ebi.ac.uk/pdbsum/2n04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n04 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DNJC5_HUMAN DNJC5_HUMAN] CLN4B disease. The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DNJC5_HUMAN DNJC5_HUMAN] May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cysteine string protein (CSP) is a member of the DnaJ/Hsp40 chaperone family that localizes to neuronal synaptic vesicles. Impaired CSP function leads to neurodegeneration in humans and model organisms as a result of misfolding of client proteins involved in neurotransmission. Mammalian CSP is phosphorylated in vivo on Ser10, and this modulates its protein interactions and effects on neurotransmitter release. However, there are no data on the structural consequences of CSP phosphorylation to explain these functional effects. We show that Ser10 phosphorylation causes an order-to-disorder transition that disrupts CSP's extreme N-terminal alpha helix. This triggers the concomitant formation of a hairpin loop stabilized by ionic interactions between phosphoSer10 and the highly conserved J-domain residue, Lys58. These phosphorylation-induced effects result in significant changes to CSP conformation and surface charge distribution. The phospho-switch revealed here provides structural insight into how Ser10 phosphorylation modulates CSP function and also has potential implications for other DnaJ phosphoproteins. | ||
| + | |||
| + | Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch.,Patel P, Prescott GR, Burgoyne RD, Lian LY, Morgan A Structure. 2016 Aug 2;24(8):1380-6. doi: 10.1016/j.str.2016.06.009. Epub 2016 Jul, 21. PMID:27452402<ref>PMID:27452402</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2n04" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Burgoyne R]] |
| - | [[Category: | + | [[Category: Lian L]] |
| - | [[Category: | + | [[Category: Morgan A]] |
| - | [[Category: | + | [[Category: Patel P]] |
| - | + | ||
Current revision
Solution Structure of the phosphorylated N-terminal region of Human Cysteine String Protein (CSP)
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