6sct: Difference between revisions
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==Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex== | |||
<SX load='6sct' size='340' side='right' viewer='molstar' caption='[[6sct]], [[Resolution|resolution]] 4.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6sct]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCT 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]] 4.69Å</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=6sct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sct OCA], [https://pdbe.org/6sct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sct RCSB], [https://www.ebi.ac.uk/pdbsum/6sct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sct ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/F1S398_PIG F1S398_PIG] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[RuleBase:RU363137] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain-heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein-protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis. | |||
Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.,Morris KL, Jones JR, Halebian M, Wu S, Baker M, Armache JP, Avila Ibarra A, Sessions RB, Cameron AD, Cheng Y, Smith CJ Nat Struct Mol Biol. 2019 Oct;26(10):890-898. doi: 10.1038/s41594-019-0292-0., Epub 2019 Oct 3. PMID:31582853<ref>PMID:31582853</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6sct" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Clathrin 3D structures|Clathrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | |||
[[Category: Cameron AD]] | |||
[[Category: Morris KL]] | |||
[[Category: Sessions R]] | |||
[[Category: Smith CJ]] | |||
Latest revision as of 16:35, 9 July 2025
Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex
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