2kj3
From Proteopedia
(Difference between revisions)
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==High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR== | ==High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR== | ||
- | <StructureSection load='2kj3' size='340' side='right' caption='[[2kj3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kj3' size='340' side='right'caption='[[2kj3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2kj3]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2kj3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Podas Podas]. The September 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Amyloids'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_9 10.2210/rcsb_pdb/mom_2015_9]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KJ3 FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rnm|2rnm]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rnm|2rnm]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">small s ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">small s ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5145 PODAS])</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kj3 OCA], [https://pdbe.org/2kj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kj3 RCSB], [https://www.ebi.ac.uk/pdbsum/2kj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kj3 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/HETS_PODAS HETS_PODAS]] Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function.<ref>PMID:1886611</ref> <ref>PMID:8224826</ref> <ref>PMID:9275200</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
- | *[[Prion|Prion]] | + | *[[Prion 3D structures|Prion 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Amyloids]] | [[Category: Amyloids]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Podas]] | [[Category: Podas]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] |
Revision as of 07:26, 14 April 2021
High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
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Categories: Amyloids | Large Structures | Podas | RCSB PDB Molecule of the Month | AB, E | Lange, A | Loquet, A | Meier, B H | Melckebeke, H Van | Wasmer, C | Amyloid fibril | Asparagine ladder | Beta-helix | Beta-solenoid | Hydrophobic core | Parallel beta-sheet | Prion | Protein fibril | Salt bridge