4ld1

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==Structural analysis of the microcephaly protein CPAP G-box domain suggests a role in centriole elongation.==
==Structural analysis of the microcephaly protein CPAP G-box domain suggests a role in centriole elongation.==
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<StructureSection load='4ld1' size='340' side='right' caption='[[4ld1]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
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<StructureSection load='4ld1' size='340' side='right'caption='[[4ld1]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ld1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LD1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ld1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.44&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ld3|4ld3]], [[4lzf|4lzf]]</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cenpj ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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=4ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld1 OCA], [https://pdbe.org/4ld1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld1 ProSAT]</span></td></tr>
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<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=4ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld1 OCA], [http://pdbe.org/4ld1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ld1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ld1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld1 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/E7FCY1_DANRE E7FCY1_DANRE]
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Centrioles are evolutionarily conserved eukaryotic organelles composed of a protein scaffold surrounded by sets of microtubules organized with a 9-fold radial symmetry. CPAP, a centriolar protein essential for microtubule recruitment, features a C-terminal domain of unknown structure, the G-box. A missense mutation in the G-box reduces affinity for the centriolar shuttling protein STIL and causes primary microcephaly. Here, we characterize the molecular architecture of CPAP and determine the G-box structure alone and in complex with a STIL fragment. The G-box comprises a single elongated beta sheet capable of forming supramolecular assemblies. Structural and biophysical studies highlight the conserved nature of the CPAP-STIL complex. We propose that CPAP acts as a horizontal "strut" that joins the centriolar scaffold with microtubules, whereas G-box domains form perpendicular connections.
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Structural Analysis of the G-Box Domain of the Microcephaly Protein CPAP Suggests a Role in Centriole Architecture.,Hatzopoulos GN, Erat MC, Cutts E, Rogala KB, Slater LM, Stansfeld PJ, Vakonakis I Structure. 2013 Sep 24. pii: S0969-2126(13)00340-7. doi:, 10.1016/j.str.2013.08.019. PMID:24076405<ref>PMID:24076405</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 4ld1" 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: Brachidanio rerio]]
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[[Category: Danio rerio]]
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[[Category: Hatzopoulos, G N]]
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[[Category: Large Structures]]
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[[Category: Vakonakis, I]]
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[[Category: Hatzopoulos GN]]
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[[Category: Beta sheet]]
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[[Category: Vakonakis I]]
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[[Category: Centriole organisation]]
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[[Category: G-box]]
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[[Category: Protein binding]]
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[[Category: Structural protein]]
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Current revision

Structural analysis of the microcephaly protein CPAP G-box domain suggests a role in centriole elongation.

PDB ID 4ld1

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