4im6
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==LRR domain from human NLRP1== | ==LRR domain from human NLRP1== | ||
| - | <StructureSection load='4im6' size='340' side='right' caption='[[4im6]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='4im6' size='340' side='right'caption='[[4im6]], [[Resolution|resolution]] 1.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4im6]] is a 1 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=4IM6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IM6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4im6]] is a 1 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=4IM6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IM6 FirstGlance]. <br> | ||
| Line 13: | Line 13: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/NALP1_HUMAN NALP1_HUMAN]] Able to form cytoplasmic structures termed death effector filaments. Enhances APAF1 and cytochrome c-dependent activation of pro-caspase-9 and consecutive apoptosis. Stimulates apoptosis through activation of caspase-3. Involved in activation of caspase-1 and caspase-5 as part of the NALP1 inflammasome complex which leads to processing and release of IL1B and IL18. Binds ATP.<ref>PMID:12191486</ref> <ref>PMID:15212762</ref> <ref>PMID:17349957</ref> | [[http://www.uniprot.org/uniprot/NALP1_HUMAN NALP1_HUMAN]] Able to form cytoplasmic structures termed death effector filaments. Enhances APAF1 and cytochrome c-dependent activation of pro-caspase-9 and consecutive apoptosis. Stimulates apoptosis through activation of caspase-3. Involved in activation of caspase-1 and caspase-5 as part of the NALP1 inflammasome complex which leads to processing and release of IL1B and IL18. Binds ATP.<ref>PMID:12191486</ref> <ref>PMID:15212762</ref> <ref>PMID:17349957</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The NOD-like receptor NLRP1 (NLR family, pyrin domain containing 1) senses the presence of the bacterial cell wall component l-muramyl dipeptide (MDP) inside the cell. We determined the crystal structure of the LRR domain of human NLRP1 in the absence of MDP to a resolution of 1.65A. The fold of the structure can be assigned to the ribonuclease inhibitor-like class of LRR proteins. We compared our structure with X-ray models of the LRR domains of NLRX1 and NLRC4 and a homology model of the LRR domain of NOD2. We conclude that the MDP binding site of NLRP1 is not located in the LRR domain. | ||
| + | |||
| + | Crystal structure of the leucine-rich repeat domain of the NOD-like receptor NLRP1: implications for binding of muramyl dipeptide.,Reubold TF, Hahne G, Wohlgemuth S, Eschenburg S FEBS Lett. 2014 Sep 17;588(18):3327-32. doi: 10.1016/j.febslet.2014.07.017. Epub , 2014 Jul 24. PMID:25064844<ref>PMID:25064844</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4im6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 18: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Eschenburg, S]] | [[Category: Eschenburg, S]] | ||
[[Category: Hahne, G]] | [[Category: Hahne, G]] | ||
Revision as of 06:07, 7 August 2019
LRR domain from human NLRP1
| |||||||||||
