6sct
From Proteopedia
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<StructureSection load='6sct' size='340' side='right'caption='[[6sct]], [[Resolution|resolution]] 4.69Å' scene=''> | <StructureSection load='6sct' size='340' side='right'caption='[[6sct]], [[Resolution|resolution]] 4.69Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6sct]] is a 15 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SCT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sct]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SCT FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6sct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sct OCA], [http://pdbe.org/6sct PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sct RCSB], [http://www.ebi.ac.uk/pdbsum/6sct PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sct ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG]), CLTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6sct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sct OCA], [http://pdbe.org/6sct PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sct RCSB], [http://www.ebi.ac.uk/pdbsum/6sct PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sct ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/C0MHR2_PIG C0MHR2_PIG]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[PIRNR:PIRNR002290] [[http://www.uniprot.org/uniprot/F1S398_PIG F1S398_PIG]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[RuleBase:RU363137] | [[http://www.uniprot.org/uniprot/C0MHR2_PIG C0MHR2_PIG]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[PIRNR:PIRNR002290] [[http://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. | ||
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| + | 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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6sct" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Pig]] | ||
[[Category: Cameron, A D]] | [[Category: Cameron, A D]] | ||
[[Category: Morris, K L]] | [[Category: Morris, K L]] | ||
Revision as of 07:44, 16 October 2019
Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex
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