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4im6

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Revision as of 06:07, 7 August 2019

LRR domain from human NLRP1

Structural highlights

4im6 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	CARD7, DEFCAP, KIAA0926, NAC, NALP1, NLRP1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[NALP1_HUMAN] Genetic variations in NLRP1 are associated with susceptibility to vitiligo (VTLG) [MIM:193200]. VTLG is a pigmentary disorder of the skin characterized by circumscribed depigmented macules and patches, commonly on extensor aspects of extremities, on the face or neck and in skin folds. It is a progressive disorder in which some or all of the melanocytes in the affected skin are selectively destroyed. It is a multifactorial disorder with a complex etiology probably including autoimmune mechanisms, and is associated with an elevated risk of other autoimmune diseases.^[1] Genetic variations in NLRP1 gene are associated with susceptibility to vitiligo-associated multiple autoimmune disease type 1 (VAMAS1) [MIM:606579]. VAMAS1 is an autoimmune disorder characterized by the association of vitiligo with several autoimmune and autoinflammatory diseases including autoimmune thyroid disease, rheumatoid arthritis and systemic lupus erythematosus.^[2]

Function

[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.^[3] ^[4] ^[5]

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^[6]

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

References

↑ Jin Y, Mailloux CM, Gowan K, Riccardi SL, LaBerge G, Bennett DC, Fain PR, Spritz RA. NALP1 in vitiligo-associated multiple autoimmune disease. N Engl J Med. 2007 Mar 22;356(12):1216-25. PMID:17377159 doi:356/12/1216
↑ Jin Y, Mailloux CM, Gowan K, Riccardi SL, LaBerge G, Bennett DC, Fain PR, Spritz RA. NALP1 in vitiligo-associated multiple autoimmune disease. N Engl J Med. 2007 Mar 22;356(12):1216-25. PMID:17377159 doi:356/12/1216
↑ Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell. 2002 Aug;10(2):417-26. PMID:12191486
↑ Liu F, Lo CF, Ning X, Kajkowski EM, Jin M, Chiriac C, Gonzales C, Naureckiene S, Lock YW, Pong K, Zaleska MM, Jacobsen JS, Silverman S, Ozenberger BA. Expression of NALP1 in cerebellar granule neurons stimulates apoptosis. Cell Signal. 2004 Sep;16(9):1013-21. PMID:15212762 doi:10.1016/j.cellsig.2004.02.006
↑ Faustin B, Lartigue L, Bruey JM, Luciano F, Sergienko E, Bailly-Maitre B, Volkmann N, Hanein D, Rouiller I, Reed JC. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell. 2007 Mar 9;25(5):713-24. PMID:17349957 doi:10.1016/j.molcel.2007.01.032
↑ Reubold TF, Hahne G, Wohlgemuth S, Eschenburg S. Crystal structure of the leucine-rich repeat domain of the NOD-like receptor NLRP1: implications for binding of muramyl dipeptide. FEBS Lett. 2014 Sep 17;588(18):3327-32. doi: 10.1016/j.febslet.2014.07.017. Epub , 2014 Jul 24. PMID:25064844 doi:http://dx.doi.org/10.1016/j.febslet.2014.07.017

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4im6"

@@ Line 1: / Line 1: @@
 ==LRR domain from human NLRP1==
-<StructureSection load='4im6' size='340' side='right' caption='[[4im6]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+<StructureSection load='4im6' size='340' side='right'caption='[[4im6]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == 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>
@@ Line 13: / Line 13: @@
 == 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>
+<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4im6" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 18: / Line 27: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Eschenburg, S]]
 [[Category: Hahne, G]]

4im6

From Proteopedia

Revision as of 06:07, 7 August 2019

LRR domain from human NLRP1

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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