View source for 4lzf


==A novel domain in the microcephaly protein CPAP suggests a role in centriole architecture==
<StructureSection load='4lzf' size='340' side='right'caption='[[4lzf]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lzf]] 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=4LZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LZF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
<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=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=4lzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lzf OCA], [https://pdbe.org/4lzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lzf RCSB], [https://www.ebi.ac.uk/pdbsum/4lzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lzf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E7FCY1_DANRE E7FCY1_DANRE] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24076405</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lzf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Cutts E]]
[[Category: Erat MC]]
[[Category: Hatzopoulos GN]]
[[Category: Rogala K]]
[[Category: Slatter L]]
[[Category: Stansfeld PJ]]
[[Category: Vakonakis I]]