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Crystal structure of the mouse innate immunity factor bacterial permeability-increasing family member A1.

Acta Crystallogr F Struct Biol Commun. 2018-01; 
LittleMichael S,RedinboMatth
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Gene Synthesis … Cloning and expression A construct for mBPIFA1 containing only amino acids 46– 278, which removes the signal sequence, was synthesized by GenScript and cloned into a pLIC expression plasmid vector with an N-terminal hexahistidine tag and a Tobacco etch virus (TEV … Get A Quote

摘要

Bacterial permeability-increasing family member A1 (BPIFA1) is an innate immunity factor and one of the most abundantly secreted proteins in the upper airways. BPIFA1 is multifunctional, with antimicrobial, surfactant and lipopolysaccharide-binding activities, as well as established roles in lung hydration. Here, the 2.5 Å resolution crystal structure of BPIFA1 from Mus musculus (mBPIFA1) is presented and compared with those of human BPIFA1 (hBPIFA1) and structural homologs. Structural distinctions between mBPIFA1 and hBPIFA1 suggest potential differences in biological function, including the regulation of a key pulmonary ion channel.

关键词

BPIFA1,Mus musculus,antimicrobial proteins,bacterial permeability-increasing family member A1,biological chemistry,innate immunity proteins,lung biology,protein surfactants,pulmonary proteins,structural biology,surfactant prot
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