Редактирование: ANTXR2 (раздел)

==Publications==

{{medline-entry
|title=Anthrax toxin receptor 2-dependent lethal toxin killing in vivo.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/17054395
|abstract=Anthrax toxin receptors 1 and 2 ([[ANTXR1]] and [[ANTXR2]]) have a related integrin-like inserted (I) domain which interacts with a metal cation that is coordinated by residue D683 of the protective antigen (PA) subunit of anthrax toxin. The receptor-bound metal ion and PA residue D683 are critical for [[ANTXR1]]-PA binding. 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]]. We show here that this is the case. The differential ability of [[ANTXR1]] and [[ANTXR2]] to bind D683 mutant PA proteins was mapped to nonconserved receptor residues at the binding interface with PA domain 2. 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.
|mesh-terms=* Animals
* Anthrax
* Antibodies, Bacterial
* Antigens, Bacterial
* Bacillus anthracis
* Bacterial Toxins
* Base Sequence
* Humans
* Longevity
* Male
* Membrane Proteins
* Microfilament Proteins
* Molecular Sequence Data
* Neoplasm Proteins
* Rats
* Rats, Inbred F344
* Receptors, Cell Surface
* Receptors, Peptide

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1617126
}}