1dfv
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CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN MONOMER
OverviewOverview
Neutrophil gelatinase associated lipocalin (NGAL), a constituent of, neutrophil granules, is a member of the lipocalin family of binding, proteins. NGAL can also be highly induced in epithelial cells in both, inflammatory and neoplastic colorectal disease. NGAL is proposed to, mediate inflammatory responses by sequestering neutrophil, chemoattractants, particularly N-formylated tripeptides and possibly, leukotriene B(4) and platelet activating factor. The crystal structures of, NGAL display a typical lipocalin fold, albeit with an unusually large and, atypically polar binding site, or calyx. The fold of NGAL is most similar, to the epididymal retinoic acid-binding protein, another lipocalin, though, the overall architecture of the calyces are very different. The crystal, structures also reveal either sulfate ions or an adventitiously copurified, fatty acid bound in the binding site. Neither ligand is displaced by added, N-formylated tripeptides. The size, shape, and character of the NGAL, calyx, as well as the low relative affinity for N-formylated tripeptides, suggest that neither the copurified fatty acid nor any of the proposed, ligands are likely to be the preferred ligand of this protein. Comparisons, between the crystal structures and the recently reported solution, structure of NGAL reveal significant differences, in terms of both the, details of the structure and the overall flexibility of the fold.
About this StructureAbout this Structure
1DFV is a Single protein structure of sequence from Homo sapiens with NDG and SO4 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin., Goetz DH, Willie ST, Armen RS, Bratt T, Borregaard N, Strong RK, Biochemistry. 2000 Feb 29;39(8):1935-41. PMID:10684642
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