4bxq
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bxq]] 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=4BXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BXQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4bxq]] 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=4BXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BXQ FirstGlance]. <br> | ||
| - | </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=4bxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bxq OCA], [https://pdbe.org/4bxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bxq RCSB], [https://www.ebi.ac.uk/pdbsum/4bxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bxq ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=4bxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bxq OCA], [https://pdbe.org/4bxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bxq RCSB], [https://www.ebi.ac.uk/pdbsum/4bxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bxq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/E7FCY1_DANRE E7FCY1_DANRE] | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Centrioles organise centrosomes and template cilia and flagella. Several centriole and centrosome proteins have been linked to microcephaly (MCPH), a neuro-developmental disease associated with small brain size. CPAP (MCPH6) and STIL (MCPH7) are required for centriole assembly, but it is unclear how mutations in them lead to microcephaly. We show that the TCP domain of CPAP constitutes a novel proline recognition domain that forms a 1:1 complex with a short, highly conserved target motif in STIL. Crystal structures of this complex reveal an unusual, all-beta structure adopted by the TCP domain and explain how a microcephaly mutation in CPAP compromises complex formation. Through point mutations, we demonstrate that complex formation is essential for centriole duplication in vivo. Our studies provide the first structural insight into how the malfunction of centriole proteins results in human disease and also reveal that the CPAP-STIL interaction constitutes a conserved key step in centriole biogenesis. DOI:http://dx.doi.org/10.7554/eLife.01071.001. | ||
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| + | Crystal structures of the CPAP/STIL complex reveal its role in centriole assembly and human microcephaly.,Cottee MA, Muschalik N, Wong YL, Johnson CM, Johnson S, Andreeva A, Oegema K, Lea SM, Raff JW, van Breugel M Elife. 2013 Sep 17;2:e01071. doi: 10.7554/eLife.01071. PMID:24052813<ref>PMID:24052813</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4bxq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of the E1021V mutant of the TCP10 domain of Danio rerio CPAP
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