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3sei

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Current revision (12:54, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3sei' size='340' side='right'caption='[[3sei]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3sei' size='340' side='right'caption='[[3sei]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sei]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SEI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sei]] is a 2 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=3SEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SEI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sen|3sen]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CASKIN1, KIAA1306 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3sei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sei OCA], [https://pdbe.org/3sei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sei RCSB], [https://www.ebi.ac.uk/pdbsum/3sei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sei 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=3sei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sei OCA], [https://pdbe.org/3sei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sei RCSB], [https://www.ebi.ac.uk/pdbsum/3sei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sei ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CSKI1_HUMAN CSKI1_HUMAN]] May link the scaffolding protein CASK to downstream intracellular effectors (By similarity).
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[https://www.uniprot.org/uniprot/CSKI1_HUMAN CSKI1_HUMAN] May link the scaffolding protein CASK to downstream intracellular effectors (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The synaptic scaffolding proteins CASK and Caskin1 are part of the fibrous mesh of proteins that organize the active zones of neural synapses. CASK binds to a region of Caskin1 called the CASK interaction domain (CID). Adjacent to the CID, Caskin1 contains two tandem sterile alpha motif (SAM) domains. Many SAM domains form polymers so they are good candidates for forming the fibrous structures seen in the active zone. We show here that the SAM domains of Caskin1 form a new type of SAM helical polymer. The Caskin1 polymer interface exhibits a remarkable segregation of charged residues, resulting in a high sensitivity to ionic strength in vitro. The Caskin1 polymers can be decorated with CASK proteins, illustrating how these proteins may work together to organize the cytomatrix in active zones.
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Tandem SAM domain structure of human Caskin1: a presynaptic, self-assembling scaffold for CASK.,Stafford RL, Hinde E, Knight MJ, Pennella MA, Ear J, Digman MA, Gratton E, Bowie JU Structure. 2011 Dec 7;19(12):1826-36. PMID:22153505<ref>PMID:22153505</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>
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<div class="pdbe-citations 3sei" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bowie, J U]]
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[[Category: Bowie JU]]
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[[Category: Stafford, R L]]
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[[Category: Stafford RL]]
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[[Category: Protein-protein interaction]]
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[[Category: Sam domain]]
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[[Category: Signaling protein]]
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Current revision

Crystal Structure of Caskin1 Tandem SAMs

PDB ID 3sei

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