INT263030

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.21
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 19
Disease Relevance 0.51
Pain Relevance 0.37

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular region (DEFB103A)
Anatomy Link Frequency
cavity 2
DEFB103A (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 122 63.84 Quite High
diclofenac 54 58.84 Quite High
cINOD 127 58.48 Quite High
psoriasis 50 50.00 Quite Low
Central nervous system 18 8.36 Low Low
cytokine 19 5.00 Very Low Very Low Very Low
cOX1 18 5.00 Very Low Very Low Very Low
Potency 18 5.00 Very Low Very Low Very Low
rheumatoid arthritis 10 5.00 Very Low Very Low Very Low
chemokine 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Alzheimer's Dementia 324 93.76 High High
Amyloidosis 144 66.80 Quite High
INFLAMMATION 140 63.84 Quite High
Disease 128 50.00 Quite Low
Psoriasis 69 50.00 Quite Low
Skin Diseases 5 47.52 Quite Low
Cardiomyopathy 72 27.56 Quite Low
Familial Amyloidotic Polyneuropathy 54 16.00 Low Low
Eczema 19 5.00 Very Low Very Low Very Low
Pressure And Volume Under Development 18 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Anti-hBD-2 antibodies were checked for specificity against hBD-2, and we found that recombinant hBD-1 (Abcam) and hBD-3 (Abcam) were not recognized.
hBD-3 Binding (recognized) of
1) Confidence 0.21 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2649503 Disease Relevance 0 Pain Relevance 0
Inhibitor 15 binds in the reverse binding mode by orienting its carboxyl substituent towards the inner binding pocket (Figures 7a and 7c) to interact with HBP3 and HBP3' near Ser117-Ser117'.
HBP3 Binding (interact) of
2) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
However, the spacer maintains two conformations (shown in magenta and green in Figures 7a and 7c) and simultaneously interacts with Ser117 and Thr119 residues of both HBP3 and HBP3' of the inner binding pocket as detailed below.
HBP3 Binding (interacts) of
3) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
However, substituents in the meta- and para- positions are not predicted to interact with HBP3 to the same extent, since they occupy the side part of this pocket.
HBP3 Binding (interact) of
4) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
When this moiety is in the meta- or para- position, these interactions with HBP3 appear to be lost, resulting in a loss of activity (cf. compounds 10 and 14 of Table 1).
HBP3 Binding (interactions) of
5) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.07 Pain Relevance 0
However, the spacer maintains two conformations (shown in magenta and green in Figures 7a and 7c) and simultaneously interacts with Ser117 and Thr119 residues of both HBP3 and HBP3' of the inner binding pocket as detailed below.
HBP3 Binding (interacts) of
6) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
Only compound 16 reveals an effective interaction with HBP3.
HBP3 Binding (interaction) of
7) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
The inner binding cavity comprises HBP3 and HBP3', formed by the side chains of Ser117, Leu110, Thr119 and Ala108 of both subunits.
HBP3 Binding (binding) of in cavity
8) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.05 Pain Relevance 0.14
15 structure, the aliphatic linker of 16 takes on two conformations with equal occupancy to simultaneously interact with both HBP3 and HBP3' residues (Figure 7b).
HBP3 Binding (interact) of
9) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
The carboxyl group simultaneously interacts with Ser117 and Thr119 residues of both HBP3 and HBP3' and facilitates a network of hydrogen bonds in the inner binding pocket connecting the Ser117 residues of all subunits, the nearby water molecules, and the carboxylate substituents of all the inhibitors.
HBP3 Binding (interacts) of
10) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
Interestingly, the hypothesized binding mode for compound 20 (Figure 8d) is different from the other inhibitors; the molecule interacts with HBP3 and HBP3' simultaneously, through the carboxylic moiety and the aminoxymethyl chain, respectively.
HBP3 Binding (interacts) of
11) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.05 Pain Relevance 0
16 structures, the tricyclic moiety of the inhibitor completely fills the outer binding pocket and the carboxylated chain adopts two conformations to interact with both the HBP3 and the HBP3' residues of the inner binding pocket.
HBP3 Binding (interact) of
12) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
The carboxyl group simultaneously interacts with Ser117 and Thr119 residues of both HBP3 and HBP3' and facilitates a network of hydrogen bonds in the inner binding pocket connecting the Ser117 residues of all subunits, the nearby water molecules, and the carboxylate substituents of all the inhibitors.
HBP3 Binding (interacts) of
13) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
Interestingly, the hypothesized binding mode for compound 20 (Figure 8d) is different from the other inhibitors; the molecule interacts with HBP3 and HBP3' simultaneously, through the carboxylic moiety and the aminoxymethyl chain, respectively.
HBP3 Binding (interacts) of
14) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.05 Pain Relevance 0
The inner binding cavity comprises HBP3 and HBP3', formed by the side chains of Ser117, Leu110, Thr119 and Ala108 of both subunits.
HBP3 Binding (binding) of in cavity
15) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.05 Pain Relevance 0.14
16 structures, the tricyclic moiety of the inhibitor completely fills the outer binding pocket and the carboxylated chain adopts two conformations to interact with both the HBP3 and the HBP3' residues of the inner binding pocket.
HBP3 Binding (interact) of
16) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
Inhibitor 15 binds in the reverse binding mode by orienting its carboxyl substituent towards the inner binding pocket (Figures 7a and 7c) to interact with HBP3 and HBP3' near Ser117-Ser117'.
HBP3 Binding (interact) of
17) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0
As shown in Figure 8e the aryl compound 24 predicted to bind in a forward binding mode while the fluorenyl analog 26 binds in the reverse binding mode (Figure 8f) with extended interactions in HBP3s and HBP1s respectively.


HBP3s Binding (interactions) of
18) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0.22 Pain Relevance 0.09
15 structure, the aliphatic linker of 16 takes on two conformations with equal occupancy to simultaneously interact with both HBP3 and HBP3' residues (Figure 7b).
HBP3 Binding (interact) of
19) Confidence 0.09 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2709434 Disease Relevance 0 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox