3qh9

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Current revision (10:47, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qh9' size='340' side='right'caption='[[3qh9]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='3qh9' size='340' side='right'caption='[[3qh9]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qh9]] is a 1 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=3QH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QH9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qh9]] 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=3QH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QH9 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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]] 2.01&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPFIBP2 ([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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=3qh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qh9 OCA], [https://pdbe.org/3qh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qh9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qh9 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=3qh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qh9 OCA], [https://pdbe.org/3qh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qh9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qh9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LIPB2_HUMAN LIPB2_HUMAN]] May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A.<ref>PMID:9624153</ref>
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[https://www.uniprot.org/uniprot/LIPB2_HUMAN LIPB2_HUMAN] May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A.<ref>PMID:9624153</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Liprins are a conserved family of scaffolding proteins important for the proper regulation and development of neuronal synapses. Humans have four liprin-alphas and two liprin-betas which all contain long coiled-coil domains followed by three tandem SAM domains. Complex interactions between the coiled-coil and SAM domains are thought to create liprin scaffolds, but the structural and biochemical properties of these domains remain largely uncharacterized. In this study we find that the human liprin-beta2 coiled-coil forms an extended dimer. Several protease-resistant subdomains within the liprin-beta1 and liprin-beta2 coiled-coils were also identified. A 2.0 A crystal structure of the central, protease-resistant core of the liprin-beta2 coiled-coil reveals a parallel helix orientation. These studies represent an initial step toward determining the overall architecture of liprin scaffolds and understanding the molecular basis for their synaptic functions.
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Crystal structure of the central coiled-coil domain from human liprin-beta2.,Stafford RL, Tang MY, Sawaya MR, Phillips ML, Bowie JU Biochemistry. 2011 May 10;50(18):3807-15. Epub 2011 Apr 15. PMID:21462929<ref>PMID:21462929</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 3qh9" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__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: Phillips, M L]]
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[[Category: Phillips ML]]
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[[Category: Stafford, R L]]
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[[Category: Stafford RL]]
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[[Category: Tang, M]]
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[[Category: Tang M]]
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[[Category: Coiled-coil]]
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[[Category: Dimerization]]
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[[Category: Structural protein]]
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Current revision

Human Liprin-beta2 Coiled-Coil

PDB ID 3qh9

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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