4ifp: Difference between revisions
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==X-ray Crystal Structure of Human NLRP1 CARD Domain== | |||
<StructureSection load='4ifp' size='340' side='right' caption='[[4ifp]], [[Resolution|resolution]] 1.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ifp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IFP FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kat|3kat]], [[3vd8|3vd8]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, b4034, JW3994, b4034, CARD7, DEFCAP, JW3994, KIAA0926, malE, NAC, NALP1, NLRP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ifp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ifp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ifp RCSB], [http://www.ebi.ac.uk/pdbsum/4ifp PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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. | [[http://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. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The NLRP1 inflammasome responds to microbial challenges such as Bacillus anthracis infection and is implicated in autoimmune disease such as vitiligo. Human NLRP1 contains both an N-terminal pyrin domain (PYD) and a C-terminal caspase recruitment domain (CARD), with the latter being essential for its association with the downstream effector procaspase-1. Here we report a 2.0 A crystal structure of the human NLRP1 CARD as a fusion with the maltose-binding protein. The structure reveals the six-helix bundle fold of the NLRP1 CARD, typical of the death domain superfamily. The charge surface of the NLRP1 CARD structure and a procaspase-1 CARD model suggests potential mechanisms for their association through electrostatic attraction. Proteins 2013. (c) 2013 Wiley Periodicals, Inc. | |||
Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1.,Jin T, Curry J, Smith P, Jiang J, Xiao TS Proteins. 2013 Mar 18. doi: 10.1002/prot.24287. PMID:23508996<ref>PMID:23508996</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Curry, J | == References == | ||
[[Category: Jiang, J | <references/> | ||
[[Category: Jin, T | __TOC__ | ||
[[Category: Smith, P | </StructureSection> | ||
[[Category: Xiao, T | [[Category: Human]] | ||
[[Category: Curry, J]] | |||
[[Category: Jiang, J]] | |||
[[Category: Jin, T]] | |||
[[Category: Smith, P]] | |||
[[Category: Xiao, T]] | |||
[[Category: Death fold superfamily]] | [[Category: Death fold superfamily]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
Revision as of 22:46, 24 December 2014
X-ray Crystal Structure of Human NLRP1 CARD Domain
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