2n05: Difference between revisions

Revision as of 08:12, 8 March 2023

Solution Structure of the non-phosphorylated N-terminal region of Human Cysteine String Protein (CSP)

Structural highlights

2n05 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

DNJC5_HUMAN CLN4B disease. The disease is caused by mutations affecting the gene represented in this entry.

Function

DNJC5_HUMAN May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Patel P, Prescott GR, Burgoyne RD, Lian LY, Morgan A. Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch. Structure. 2016 Aug 2;24(8):1380-6. doi: 10.1016/j.str.2016.06.009. Epub 2016 Jul, 21. PMID:27452402 doi:https://dx.doi.org/10.1016/j.str.2016.06.009

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Patel P, Prescott GR, Burgoyne RD, Lian LY, Morgan A. Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch. Structure. 2016 Aug 2;24(8):1380-6. doi: 10.1016/j.str.2016.06.009. Epub 2016 Jul, 21. PMID:27452402 doi:https://dx.doi.org/10.1016/j.str.2016.06.009

[1]

@@ Line 1: / Line 1: @@
 ==Solution Structure of the non-phosphorylated N-terminal region of Human Cysteine String Protein (CSP)==
-<StructureSection load='2n05' size='340' side='right'caption='[[2n05]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2n05' size='340' side='right'caption='[[2n05]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2n05]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N05 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2n05]] 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=2N05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N05 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNAJC5, CSP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=2n05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n05 OCA], [https://pdbe.org/2n05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n05 RCSB], [https://www.ebi.ac.uk/pdbsum/2n05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n05 ProSAT]</span></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=2n05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n05 OCA], [https://pdbe.org/2n05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n05 RCSB], [https://www.ebi.ac.uk/pdbsum/2n05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n05 ProSAT]</span></td></tr>
 </table>
 == 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.
+[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 ==
-[[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).
+[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 ==
@@ Line 27: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Burgoyne, R]]
+[[Category: Burgoyne R]]
-[[Category: Lian, L]]
+[[Category: Lian L]]
-[[Category: Morgan, A]]
+[[Category: Morgan A]]
-[[Category: Patel, P]]
+[[Category: Patel P]]
-[[Category: Chaperone]]
-[[Category: Dnaj]]
-[[Category: Phosphorylation]]

2n05: Difference between revisions

Revision as of 08:12, 8 March 2023

Solution Structure of the non-phosphorylated N-terminal region of Human Cysteine String Protein (CSP)

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

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