4by2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4by2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BY2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4by2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BY2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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]] 2.57Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4by2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4by2 OCA], [https://pdbe.org/4by2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4by2 RCSB], [https://www.ebi.ac.uk/pdbsum/4by2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4by2 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=4by2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4by2 OCA], [https://pdbe.org/4by2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4by2 RCSB], [https://www.ebi.ac.uk/pdbsum/4by2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4by2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q9XZ31_DROME Q9XZ31_DROME] [https://www.uniprot.org/uniprot/Q9VI72_DROME Q9VI72_DROME] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4by2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 14:06, 9 May 2024
SAS-4 (dCPAP) TCP domain in complex with a Proline Rich Motif of Ana2 (dSTIL) of Drosophila MelanogasterSAS-4 (dCPAP) TCP domain in complex with a Proline Rich Motif of Ana2 (dSTIL) of Drosophila Melanogaster
Structural highlights
FunctionPublication Abstract from PubMedCentrioles 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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