4ikm

From Proteopedia

(Difference between revisions)

Current revision

X-ray structure of CARD8 CARD domain

Structural highlights

4ikm is a 1 chain structure with sequence from Escherichia coli K-12 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4606Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.CARD8_HUMAN Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases.

Publication Abstract from PubMed

CARD8 plays crucial roles in regulating apoptotic and inflammatory signaling pathways through the association of its caspase-recruitment domain (CARD) with those of procaspase-9 and procaspase-1. The CARD8 CARD has also been predicted to form an intramolecular complex with its FIIND domain. Here, the first crystal structure of the CARD8 CARD is reported; it adopts a six-helix bundle fold with a unique conformation of the alpha6 helix that is described here for the first time. The surface of the CARD8 CARD displays a prominent acidic patch at its alpha2, alpha3 and alpha5 helices that may interact with the procaspase-9 CARD, whereas an adjacent charged surface at its alpha3 and alpha4 helices may associate with the CARD8 FIIND domain without interfering with the CARD-CARD interaction. This suggests that the function of CARD8 may be regulated by both intramolecular and intermolecular interactions involving electrostatic attractions.

The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces.,Jin T, Huang M, Smith P, Jiang J, Xiao TS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):482-7. doi:, 10.1107/S1744309113010075. Epub 2013 Apr 27. PMID:23695559^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jin T, Huang M, Smith P, Jiang J, Xiao TS. The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):482-7. doi:, 10.1107/S1744309113010075. Epub 2013 Apr 27. PMID:23695559 doi:10.1107/S1744309113010075

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ikm"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4ikm is ON HOLD
+==X-ray structure of CARD8 CARD domain==
+<StructureSection load='4ikm' size='340' side='right'caption='[[4ikm]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ikm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IKM FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4606&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</scene></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=4ikm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ikm OCA], [https://pdbe.org/4ikm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ikm RCSB], [https://www.ebi.ac.uk/pdbsum/4ikm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ikm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/CARD8_HUMAN CARD8_HUMAN] Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CARD8 plays crucial roles in regulating apoptotic and inflammatory signaling pathways through the association of its caspase-recruitment domain (CARD) with those of procaspase-9 and procaspase-1. The CARD8 CARD has also been predicted to form an intramolecular complex with its FIIND domain. Here, the first crystal structure of the CARD8 CARD is reported; it adopts a six-helix bundle fold with a unique conformation of the alpha6 helix that is described here for the first time. The surface of the CARD8 CARD displays a prominent acidic patch at its alpha2, alpha3 and alpha5 helices that may interact with the procaspase-9 CARD, whereas an adjacent charged surface at its alpha3 and alpha4 helices may associate with the CARD8 FIIND domain without interfering with the CARD-CARD interaction. This suggests that the function of CARD8 may be regulated by both intramolecular and intermolecular interactions involving electrostatic attractions.
-Authors: Tengchuan Jin, Mo Huang, Patrick Smith, Jiansheng Jiang, Tsan Xiao
+The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces.,Jin T, Huang M, Smith P, Jiang J, Xiao TS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):482-7. doi:, 10.1107/S1744309113010075. Epub 2013 Apr 27. PMID:23695559<ref>PMID:23695559</ref>
-Description: X-ray structure of CARD8 CARD domain
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4ikm" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Huang M]]
+[[Category: Jiang J]]
+[[Category: Jin T]]
+[[Category: Smith P]]
+[[Category: Xiao T]]

4ikm

From Proteopedia

Current revision

X-ray structure of CARD8 CARD domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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