INT198144

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Context Info
Confidence 0.00
First Reported 2006
Last Reported 2006
Negated 1
Speculated 1
Reported most in Body
Documents 1
Total Number 9
Disease Relevance 3.40
Pain Relevance 0

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

pigmentation (PLDN) cytosol (PLDN) endosome (PLDN)
extracellular region (ANTXR2) endoplasmic reticulum (ANTXR2) plasma membrane (ANTXR2)
PLDN (Homo sapiens)
ANTXR2 (Homo sapiens)
PLDN - D683K (1)
Pain Link Frequency Relevance Heat
addiction 9 17.84 Low Low
anesthesia 9 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Bacillus Anthracis Infection 153 98.84 Very High Very High Very High
Poisoning 171 96.08 Very High Very High Very High
Death 90 81.40 Quite High
Disease 27 76.72 Quite High
Adhesions 9 73.76 Quite High
Cancer 27 63.12 Quite High
Diphtheria 9 43.24 Quite Low
Pressure And Volume Under Development 18 34.16 Quite Low
Infection 9 5.92 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Since PA can bind to ANTXR2 with reduced affinity in the absence of metal ions, we reasoned that D683 mutant forms of PA might specifically interact with ANTXR2.
PA Spec (might) Binding (interact) of ANTXR2
1) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Abstract Doc Link PMC1617126 Disease Relevance 0.56 Pain Relevance 0
To address the possible role of ANTXR2 in lethal toxin killing of Fischer 344 rats, we first confirmed that D683 mutant forms of PA can interact with rat ANTXR2 (rANTXR2) but not rat ANTXR1.
PA Neg (not) Binding (interact) of ANTXR2
2) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1617126 Disease Relevance 0.33 Pain Relevance 0
This report demonstrates that D683 mutant forms of PA bind selectively to ANTXR2 and that this selectivity is dependent on amino acid residues of ANTXR2 that contact domain 2 of PA.
PA Binding (bind) of ANTXR2
3) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1617126 Disease Relevance 0.23 Pain Relevance 0
Based on the co-crystal structures of ANTXR2 bound to PA (Figure 1), there are eight contact residues that would be different at the toxin-binding interface in ANTXR1: A56L, N57H, Q88R, S113L, V115G, D152H, G153E, and L154D [31,32] (Figure S1).
PA Binding (bound) of ANTXR2
4) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1617126 Disease Relevance 0.08 Pain Relevance 0
The large contact surface correlates with a very tight ANTXR2 I domain–PA binding affinity (KD = 170 or 780 pM in Mg2+ or Ca2+, respectively) [35], compared with the affinity of ?
PA Binding (affinity) of ANTXR2
5) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1617126 Disease Relevance 0.46 Pain Relevance 0
Replacing the ANTXR2 G153, which allows a polypeptide backbone turn, and L154, which participates in hydrophobic interactions with PA, with the negatively charged Glu and Asp residues from ANTXR1 resulted in resistance to cellular intoxication with PAD683N.
PA Binding (interactions) of ANTXR2 associated with poisoning
6) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1617126 Disease Relevance 0.30 Pain Relevance 0
The hANTXR2 R111 residue interacts with a negatively charged environment in PA domain 4, and the S113 residue makes H-bond contacts with PA domain 4 in the crystal structure (unpublished data) [31,32].
PA Binding (interacts) of hANTXR2
7) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1617126 Disease Relevance 0.29 Pain Relevance 0
Moreover, a D683K mutant form of PA that bound specifically to human and rat ANTXR2 mediated killing of rats by anthrax lethal toxin, providing strong evidence for the physiological importance of ANTXR2 in anthrax disease pathogenesis.


PA (D683K) Binding (bound) of ANTXR2 associated with bacillus anthracis infection
8) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Abstract Doc Link PMC1617126 Disease Relevance 0.72 Pain Relevance 0
Since PA can bind to ANTXR2 with reduced affinity in the absence of metal ions, we reasoned that D683 mutant forms of PA might specifically interact with ANTXR2.
PA Binding (bind) of ANTXR2
9) Confidence 0.00 Published 2006 Journal PLoS Pathogens Section Abstract Doc Link PMC1617126 Disease Relevance 0.43 Pain Relevance 0

General Comments

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