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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.== |
- | <StructureSection load='4ld3' size='340' side='right' caption='[[4ld3]], [[Resolution|resolution]] 2.44Å' scene=''> | + | <StructureSection load='4ld3' size='340' side='right'caption='[[4ld3]], [[Resolution|resolution]] 2.44Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4ld3]] is a 2 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=4LD3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LD3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ld3]] is a 2 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=4LD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD3 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> | + | </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=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ld1|4ld1]], [[4lzf|4lzf]]</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=4ld3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld3 OCA], [https://pdbe.org/4ld3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld3 ProSAT]</span></td></tr> |
- | <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]), stil, sill, zgc:110502 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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=4ld3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld3 OCA], [http://pdbe.org/4ld3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ld3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ld3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld3 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/STIL_DANRE STIL_DANRE]] Plays an essential role in early embryonic development. | + | [https://www.uniprot.org/uniprot/E7FCY1_DANRE E7FCY1_DANRE] |
| <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: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
- | [[Category: Hatzopoulos, G N]] | + | [[Category: Large Structures]] |
- | [[Category: Vakonakis, I]] | + | [[Category: Hatzopoulos GN]] |
- | [[Category: Beta-sheet]] | + | [[Category: Vakonakis I]] |
- | [[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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| Structural highlights
Function
E7FCY1_DANRE
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hatzopoulos GN, Erat MC, Cutts E, Rogala KB, Slater LM, Stansfeld PJ, Vakonakis I. Structural Analysis of the G-Box Domain of the Microcephaly Protein CPAP Suggests a Role in Centriole Architecture. Structure. 2013 Sep 24. pii: S0969-2126(13)00340-7. doi:, 10.1016/j.str.2013.08.019. PMID:24076405 doi:http://dx.doi.org/10.1016/j.str.2013.08.019
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