6BAQ
Mus musculus BPIFA1
Summary for 6BAQ
Entry DOI | 10.2210/pdb6baq/pdb |
Descriptor | BPI fold-containing family A member 1, SODIUM ION, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | antimicrobial protein, lung defense protein, surfactant protein, lipid binding protein |
Biological source | Mus musculus (Mouse) |
Total number of polymer chains | 8 |
Total formula weight | 203640.84 |
Authors | Little, M.S.,Redinbo, M.R. (deposition date: 2017-10-15, release date: 2018-05-09, Last modification date: 2024-10-16) |
Primary citation | Little, M.S.,Redinbo, M.R. Crystal structure of the mouse innate immunity factor bacterial permeability-increasing family member A1. Acta Crystallogr F Struct Biol Commun, 74:268-276, 2018 Cited by PubMed Abstract: 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. PubMed: 29717993DOI: 10.1107/S2053230X18004600 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.50260996677 Å) |
Structure validation
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