View source for 8bda


==IFTA complex in anterograde intraflagellar transport trains (Chlamydomonas reinhardtii)==
<StructureSection load='8bda' size='340' side='right'caption='[[8bda]], [[Resolution|resolution]] 20.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8bda]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BDA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 20.7&#8491;</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=8bda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bda OCA], [https://pdbe.org/8bda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bda RCSB], [https://www.ebi.ac.uk/pdbsum/8bda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bda ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8JFR3_CHLRE A8JFR3_CHLRE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Anterograde intraflagellar transport (IFT) trains are essential for cilia assembly and maintenance. These trains are formed of 22 IFT-A and IFT-B proteins that link structural and signaling cargos to microtubule motors for import into cilia. It remains unknown how the IFT-A/-B proteins are arranged into complexes and how these complexes polymerize into functional trains. Here we use in situ cryo-electron tomography of Chlamydomonas reinhardtii cilia and AlphaFold2 protein structure predictions to generate a molecular model of the entire anterograde train. We show how the conformations of both IFT-A and IFT-B are dependent on lateral interactions with neighboring repeats, suggesting that polymerization is required to cooperatively stabilize the complexes. Following three-dimensional classification, we reveal how IFT-B extends two flexible tethers to maintain a connection with IFT-A that can withstand the mechanical stresses present in actively beating cilia. Overall, our findings provide a framework for understanding the fundamental processes that govern cilia assembly.

The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.,Lacey SE, Foster HE, Pigino G Nat Struct Mol Biol. 2023 May;30(5):584-593. doi: 10.1038/s41594-022-00905-5. , Epub 2023 Jan 2. PMID:36593313<ref>PMID:36593313</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8bda" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Foster HE]]
[[Category: Lacey SE]]
[[Category: Pigino G]]