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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 | <StructureSection load='2kj3' size='340' side='right'caption='[[2kj3]]' 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/Podospora_anserina Podospora anserina]. 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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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> | ||
==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: | [[Category: Large Structures]] | ||
[[Category: Podospora anserina]] | |||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: | [[Category: AB E]] | ||
[[Category: Lange | [[Category: Lange A]] | ||
[[Category: Loquet | [[Category: Loquet A]] | ||
[[Category: Meier | [[Category: Meier BH]] | ||
[[Category: Melckebeke | [[Category: Van Melckebeke H]] | ||
[[Category: Wasmer | [[Category: Wasmer C]] | ||
Latest revision as of 09:46, 1 May 2024
High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMRHigh-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
Structural highlights
FunctionHETS_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.[1] [2] [3] See AlsoReferences
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