6j52

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6j52 is ON HOLD until Paper Publication
+
==Crystal structure of CARD-only protein in frog virus 3==
 +
<StructureSection load='6j52' size='340' side='right' caption='[[6j52]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6j52]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J52 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=6j52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j52 OCA], [http://pdbe.org/6j52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j52 RCSB], [http://www.ebi.ac.uk/pdbsum/6j52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j52 ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Caspase recruitment domain (CARD)-only proteins (COPs), regulate apoptosis, inflammation, and innate immunity. They inhibit the assembly of NOD-like receptor complexes such as the inflammasome and NODosome, which are molecular complexes critical for caspase-1 activation. COPs are known to interact with either caspase-1 CARD or RIP2 CARD via a CARD-CARD interaction, and inhibit caspase-1 activation or further downstream signaling. In addition to the human COPs, Pseudo-ICE, INCA, and ICEBERG, several viruses also contain viral COPs that help them escape the host immune system. To elucidate the molecular mechanism of host immunity inhibition by viral COPs, we solved the structure of a viral COP for the first time. Our structure showed that viral COP forms a structural transformation-mediated dimer, which is unique and has not been reported in any structural study of a CARD domain. Based on the current structure, and the previously solved structures of other death domain superfamily members, we propose that structural transformation-mediated dimerization might be a new strategy for dimer assembly in the death domain superfamily.
-
Authors:
+
Structural transformation-mediated dimerization of caspase recruitment domain revealed by the crystal structure of CARD-only protein in frog virus 3.,Kim CM, Ha HJ, Kwon S, Jeong JH, Lee SH, Kim YG, Lee CS, Lee JH, Park HH J Struct Biol. 2019 Jan 6. pii: S1047-8477(19)30001-2. doi:, 10.1016/j.jsb.2018.12.006. PMID:30625366<ref>PMID:30625366</ref>
-
Description:
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 6j52" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Kwon, S]]
 +
[[Category: Park, H H]]
 +
[[Category: Apoptosis]]
 +
[[Category: Card-only protein]]
 +
[[Category: Caspase recruitment domain]]
 +
[[Category: Death domain superfamily]]
 +
[[Category: Domain swapping]]

Revision as of 06:50, 21 February 2019

Crystal structure of CARD-only protein in frog virus 3

6j52, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools