1L6M

Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition

1L6M の概要

• エントリーDOI: 10.2210/pdb1l6m/pdb
• 関連するPDBエントリー: 1dfv 1qqs
• 分子名称: Neutrophil gelatinase-associated lipocalin, FE (III) ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: lipocalin, siderophore, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P80188
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 64051.61

構造登録者

Goetz, D.H.,Borregaard, N.,Bluhm, M.E.,Raymond, K.N.,Strong, R.K. (登録日: 2002-03-11, 公開日: 2003-03-11, 最終更新日: 2024-10-16)

主引用文献

Goetz, D.H.,Borregaard, N.,Bluhm, M.E.,Raymond, K.N.,Strong, R.K.
The Neutrophil Lipocalin NGAL is a Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition
Mol.Cell, 10:1033-1043, 2002

PubMed Abstract: First identified as a neutrophil granule component, neutrophil gelatinase-associated lipocalin (NGAL; also called human neutrophil lipocalin, 24p3, uterocalin, or neu-related lipocalin) is a member of the lipocalin family of binding proteins. Putative NGAL ligands, including neutrophil chemotactic agents such as N-formylated tripeptides, have all been refuted by recent biochemical and structural results. NGAL has subsequently been implicated in diverse cellular processes, but without a characterized ligand, the molecular basis of these functions remained mysterious. Here we report that NGAL tightly binds bacterial catecholate-type ferric siderophores through a cyclically permuted, hybrid electrostatic/cation-pi interaction and is a potent bacteriostatic agent in iron-limiting conditions. We therefore propose that NGAL participates in the antibacterial iron depletion strategy of the innate immune system.

PubMed: 12453412
DOI: 10.1016/S1097-2765(02)00708-6

実験手法

X-RAY DIFFRACTION (2.4 Å)