|Entry||Database: PDB / ID: 1pn5|
|Title||NMR structure of the NALP1 Pyrin domain (PYD)|
|Components||NACHT-, LRR- and PYD-containing protein 2|
|Keywords||APOPTOSIS / 5 ALPHA-HELIX BUNDLE|
|Function / homology|
Function and homology information
NLRP1 inflammasome complex assembly / cysteine-type endopeptidase activator activity / NLRP1 inflammasome complex / inflammasome complex / self proteolysis / antiviral innate immune response / pattern recognition receptor signaling pathway / The NLRP1 inflammasome / Hydrolases; Acting on peptide bonds (peptidases) / pyroptosis ...NLRP1 inflammasome complex assembly / cysteine-type endopeptidase activator activity / NLRP1 inflammasome complex / inflammasome complex / self proteolysis / antiviral innate immune response / pattern recognition receptor signaling pathway / The NLRP1 inflammasome / Hydrolases; Acting on peptide bonds (peptidases) / pyroptosis / cysteine-type endopeptidase activator activity involved in apoptotic process / IgG binding / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / response to muramyl dipeptide / positive regulation of interleukin-1 beta production / protein homooligomerization / positive regulation of inflammatory response / activation of cysteine-type endopeptidase activity involved in apoptotic process / protein self-association / neuron apoptotic process / double-stranded RNA binding / regulation of inflammatory response / double-stranded DNA binding / defense response to virus / peptidase activity / endopeptidase activity / regulation of apoptotic process / inflammatory response / defense response to bacterium / protein domain specific binding / apoptotic process / nucleolus / ATP hydrolysis activity / enzyme binding / extracellular region / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
FIIND domain profile. / FIIND domain / Function to find / CARD8/ASC/NALP1, CARD domain / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / NOD2 winged helix domain / NOD2, winged helix domain / NACHT nucleoside triphosphatase / NACHT-NTPase domain profile. ...FIIND domain profile. / FIIND domain / Function to find / CARD8/ASC/NALP1, CARD domain / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / NOD2 winged helix domain / NOD2, winged helix domain / NACHT nucleoside triphosphatase / NACHT-NTPase domain profile. / NACHT domain / DAPIN domain / DAPIN domain profile. / PAAD/DAPIN/Pyrin domain / PAAD/DAPIN/Pyrin domain / B domain / IgG-binding B / Death Domain, Fas / Death Domain, Fas / M protein-type anchor domain / GA-like domain / GA-like domain / Leucine Rich repeat / Immunoglobulin/albumin-binding domain superfamily / CARD caspase recruitment domain profile. / CARD domain / Caspase recruitment domain / YSIRK Gram-positive signal peptide / LPXTG cell wall anchor motif / Gram-positive cocci surface proteins LPxTG motif profile. / LPXTG cell wall anchor domain / Leucine-rich repeat profile. / Death-like domain superfamily / Leucine-rich repeat / Leucine-rich repeat domain superfamily / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Immunoglobulin G-binding protein G / NACHT, LRR and PYD domains-containing protein 1
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||SOLUTION NMR / torsion angle dynamics|
|Authors||Hiller, S. / Kohl, A. / Fiorito, F. / Herrmann, T. / Wider, G. / Tschopp, J. / Grutter, M.G. / Wuthrich, K.|
|Citation||Journal: Structure / Year: 2003|
Title: NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain
Authors: Hiller, S. / Kohl, A. / Fiorito, F. / Herrmann, T. / Wider, G. / Tschopp, J. / Grutter, M.G. / Wuthrich, K.
|Remark 999||SEQUENCE Residues 1-58 are missing from the coordinates because they were not included in the model. ...SEQUENCE Residues 1-58 are missing from the coordinates because they were not included in the model. Residues 57 and 58 are independent linking residues, which have been inserted to provide distance and flexibiltiy in this two-domain fusion protein.|
|Remark 650||HELIX Determination method: author|
|Structure viewer||Molecule: |
Downloads & links
A: NACHT-, LRR- and PYD-containing protein 2
|#1: Protein|| |
Mass: 17680.607 Da / Num. of mol.: 1 / Fragment: Pyrin domain (PYD)
Source method: isolated from a genetically manipulated source
Details: Residues 1-56 correspond to the fused Immunoglobulin G binding protein G (SWS P06654, residues 228-282)
Source: (gene. exp.) Homo sapiens (human) / Gene: NALP1 / Plasmid: pET20b+ / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P06654, UniProt: Q9C000
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: Protein was expressed as a fusion protein with G B1 to enhance solubility (Zhou et al., J. Biomol. NMR 20, 11-14)|
|Details||Contents: 1mM NALP1 PYD U-15N,13C; 50mM Na / PO4 - Buffer; 50mM NaCl; 1mM CHAPS; 20mM DTT (D10); 0.02% NaN3; 0.1mM EDTA; protease inhibitor cocktail (Complete, Roche); 95% H2O, 5% D2O|
Solvent system: 95% H2O/5% D2O
|Sample conditions||pH: 6.5 / Pressure: 1 atm / Temperature: 293 K|
*PLUSMethod: other / Details: NMR
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|Refinement||Method: torsion angle dynamics / Software ordinal: 1|
|NMR representative||Selection criteria: aesthetic reasons|
|NMR ensemble||Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20|
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