A,B,C—overlay of the structures in ribbon representation. B demonstrates the different conformation of the P518 peptide bond. C shows the differences in the positions of charged residues in H1. D—structure of RIP2CARD with indicated and assigned residues that are important for the proper packing of C-terminal residues.</p
<p>A. Consensus sequences of RBDs 1–6. The conserved residues are ordered according to frequency, wi...
<p>(A) Table of sequence identity and similarity of the cathelin-like domain from diverse groups of ...
Solid grey bars give the RMSF for four peptides – excluding R18 – and the hatched bars give the RMSF...
At top, the aminoacid sequences of homologous to the rat RIP2 RIPK2 proteins are aligned with RIP2CA...
RIP2, one of the RIP kinases, interacts with p75 neurotrophin receptor, regulating the neuron surviv...
A—20 best structures of the stable core of RIP2CARD (432–524) are superimposed over the backbone ato...
Conserved hydrophobic core residues are indicated by *, and totally conserved residues by #. The blu...
<p>(A) Structure of the CARD-CARD complex between Apaf-1 (light blue) and procaspase-9 (yellow), pdb...
PRRs play an essential role in detecting pathogenic infections and propagating such immune signals t...
PRRs play an essential role in detecting pathogenic infections and propagating such immune signals t...
<p>(A) The NMR structure of mouse Mesd C-terminal domain (155–191) based on the study of Chen et al....
<p><b>*</b>Shown are tyrosine sites within the CARD of RIP2 <b>(<u>r</u></b>eceptor <b><u>i</u></b>n...
<p>Different secondary structure elements are drawn in different colours (purple: α-helix, yellow: β...
The maps of electrostatic potential distribution on the Van-der-Waals surface of NOD1 CARD (on top) ...
Domains are coloured according to the linear sequence scheme shown above the ribbon diagram. Structu...
<p>A. Consensus sequences of RBDs 1–6. The conserved residues are ordered according to frequency, wi...
<p>(A) Table of sequence identity and similarity of the cathelin-like domain from diverse groups of ...
Solid grey bars give the RMSF for four peptides – excluding R18 – and the hatched bars give the RMSF...
At top, the aminoacid sequences of homologous to the rat RIP2 RIPK2 proteins are aligned with RIP2CA...
RIP2, one of the RIP kinases, interacts with p75 neurotrophin receptor, regulating the neuron surviv...
A—20 best structures of the stable core of RIP2CARD (432–524) are superimposed over the backbone ato...
Conserved hydrophobic core residues are indicated by *, and totally conserved residues by #. The blu...
<p>(A) Structure of the CARD-CARD complex between Apaf-1 (light blue) and procaspase-9 (yellow), pdb...
PRRs play an essential role in detecting pathogenic infections and propagating such immune signals t...
PRRs play an essential role in detecting pathogenic infections and propagating such immune signals t...
<p>(A) The NMR structure of mouse Mesd C-terminal domain (155–191) based on the study of Chen et al....
<p><b>*</b>Shown are tyrosine sites within the CARD of RIP2 <b>(<u>r</u></b>eceptor <b><u>i</u></b>n...
<p>Different secondary structure elements are drawn in different colours (purple: α-helix, yellow: β...
The maps of electrostatic potential distribution on the Van-der-Waals surface of NOD1 CARD (on top) ...
Domains are coloured according to the linear sequence scheme shown above the ribbon diagram. Structu...
<p>A. Consensus sequences of RBDs 1–6. The conserved residues are ordered according to frequency, wi...
<p>(A) Table of sequence identity and similarity of the cathelin-like domain from diverse groups of ...
Solid grey bars give the RMSF for four peptides – excluding R18 – and the hatched bars give the RMSF...