2BJJ

Structure of recombinant human lactoferrin produced in the milk of transgenic cows

2BJJ の概要

• エントリーDOI: 10.2210/pdb2bjj/pdb
• 関連するPDBエントリー: 1B0L 1BKA 1CB6 1DSN 1EH3 1FCK 1H43 1H44 1H45 1HSE 1L5T 1LCF 1LCT 1LFG 1LFH 1LFI 1LGB 1N76 1SQY 1VFD 1VFE
• 分子名称: LACTOTRANSFERRIN, FE (III) ION, CARBONATE ION, ... (5 entities in total)
• 機能のキーワード: metal-binding protein, lactoferrin, transgenic cows, iron-binding, antibiotic, glycoprotein, polymorphism, metal binding protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 77108.57

構造登録者

Thomassen, E.A.J.,Van Veen, H.A.,Van Berkel, P.H.C.,Nuijens, J.H.,Abrahams, J.P. (登録日: 2005-02-03, 公開日: 2005-08-01, 最終更新日: 2024-11-06)

主引用文献

Thomassen, E.A.J.,Van Veen, H.A.,Van Berkel, P.H.C.,Nuijens, J.H.,Abrahams, J.P.
The Protein Structure of Recombinant Human Lactoferrin Produced in the Milk of Transgenic Cows Closely Matches the Structure of Human Milk-Derived Lactoferrin
Transgenic Res., 14:397-, 2005

PubMed Abstract: Human lactoferrin (hLF) is an iron-binding glycoprotein involved in the host defence against infection and excessive inflammation. As the availability of (human milk-derived) natural hLF is limited, alternative means of production of this biopharmaceutical are extensively researched. Here we report the crystal structure of recombinant hLF (rhLF) expressed in the milk of transgenic cows at a resolution of 2.4 A. To our knowledge, the first reported structure of a recombinant protein produced in milk of transgenic livestock. Even though rhLF contains oligomannose- and hybrid-type N-linked glycans next to complex-type glycans, which are the only glycans found on natural hLF, the structures are identical within the experimental error (r.m.s. deviation of only 0.28 A for the main-chain atoms). Of the differences in polymorphic amino acids between the natural and rhLF variant used, only the side-chain of Asp561 could be modeled into the rhLF electron density map. Taken together, the results confirm the structural integrity of the rhLF variant used in this study. It also confirms the validity of the transgenic cow mammary gland as a vehicle to produce recombinant human proteins.

PubMed: 16201406
DOI: 10.1007/S11248-005-3233-0

実験手法

X-RAY DIFFRACTION (2.4 Å)