2kj3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 2kj3 is ON HOLD Authors: Van Melckebeke, H., Wasmer, C., Lange, A., AB, E., Loquet, A., Meier, B.H. Description: HIGH-RESOLUTION STRUCTURE OF THE H...)
Current revision (06:46, 1 May 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 2kj3 is ON HOLD
+
==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]]' scene=''>
 +
== Structural highlights ==
 +
<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='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>
 +
</table>
 +
== 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>
-
Authors: Van Melckebeke, H., Wasmer, C., Lange, A., AB, E., Loquet, A., Meier, B.H.
+
==See Also==
-
 
+
*[[Prion 3D structures|Prion 3D structures]]
-
Description: HIGH-RESOLUTION STRUCTURE OF THE HET-S(218-289) PRION IN ITS AMYLOID FORM OBTAINED BY SOLID-STATE NMR
+
== References ==
-
 
+
<references/>
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 27 14:23:50 2009''
+
__TOC__
 +
</StructureSection>
 +
[[Category: Amyloids]]
 +
[[Category: Large Structures]]
 +
[[Category: Podospora anserina]]
 +
[[Category: RCSB PDB Molecule of the Month]]
 +
[[Category: AB E]]
 +
[[Category: Lange A]]
 +
[[Category: Loquet A]]
 +
[[Category: Meier BH]]
 +
[[Category: Van Melckebeke H]]
 +
[[Category: Wasmer C]]

Current revision

High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

PDB ID 2kj3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools