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| | ==CASKIN2 SAM domain tandem== | | ==CASKIN2 SAM domain tandem== |
| - | <StructureSection load='5l1m' size='340' side='right' caption='[[5l1m]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <StructureSection load='5l1m' size='340' side='right'caption='[[5l1m]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l1m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L1M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L1M FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CASKIN2, KIAA1139 ([http://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=5l1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l1m OCA], [https://pdbe.org/5l1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l1m RCSB], [https://www.ebi.ac.uk/pdbsum/5l1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l1m ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l1m OCA], [http://pdbe.org/5l1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l1m RCSB], [http://www.ebi.ac.uk/pdbsum/5l1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l1m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CSKI2_HUMAN CSKI2_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Donaldson, L W]] | + | [[Category: Large Structures]] |
| - | [[Category: Kwan, J J]] | + | [[Category: Donaldson LW]] |
| - | [[Category: Saridakis, V]] | + | [[Category: Kwan JJ]] |
| - | [[Category: Protein binding]] | + | [[Category: Saridakis V]] |
| - | [[Category: Protein interaction domain]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Sterile alpha motif]]
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| Structural highlights
Function
CSKI2_HUMAN
Publication Abstract from PubMed
BACKGROUND: CASKIN2 is a homolog of CASKIN1, a scaffolding protein that participates in a signaling network with CASK (calcium/calmodulin-dependent serine kinase). Despite a high level of homology between CASKIN2 and CASKIN1, CASKIN2 cannot bind CASK due to the absence of a CASK Interaction Domain and consequently, may have evolved undiscovered structural and functional distinctions. RESULTS: We demonstrate that the crystal structure of the Sterile Alpha Motif (SAM) domain tandem (SAM1-SAM2) oligomer from CASKIN2 is different than CASKIN1, with the minimal repeating unit being a dimer, rather than a monomer. Analytical ultracentrifugation sedimentation velocity methods revealed differences in monomer/dimer equilibria across a range of concentrations and ionic strengths for the wild type CASKIN2 SAM tandem and a structure-directed double mutant that could not oligomerize. Further distinguishing CASKIN2 from CASKIN1, EGFP-tagged SAM tandem proteins expressed in Neuro2a cells produced punctae that were distinct both in shape and size. CONCLUSIONS: This study illustrates a new way in which neuronal SAM domains can assemble into large macromolecular assemblies that might concentrate and amplify synaptic responses.
A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein.,Smirnova E, Kwan JJ, Siu R, Gao X, Zoidl G, Demeler B, Saridakis V, Donaldson LW Cell Commun Signal. 2016 Aug 22;14(1):17. doi: 10.1186/s12964-016-0140-3. PMID:27549312[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Smirnova E, Kwan JJ, Siu R, Gao X, Zoidl G, Demeler B, Saridakis V, Donaldson LW. A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein. Cell Commun Signal. 2016 Aug 22;14(1):17. doi: 10.1186/s12964-016-0140-3. PMID:27549312 doi:http://dx.doi.org/10.1186/s12964-016-0140-3
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