1B0L

RECOMBINANT HUMAN DIFERRIC LACTOFERRIN

1B0L の概要

• エントリーDOI: 10.2210/pdb1b0l/pdb
• 分子名称: PROTEIN (LACTOFERRIN), FE (III) ION, CARBONATE ION, ... (4 entities in total)
• 機能のキーワード: transferrin, binding protein, metalloprotein, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P02788
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76525.00

構造登録者

Baker, E.N.,Jameson, G.B.,Sun, X. (登録日: 1998-11-11, 公開日: 1999-11-18, 最終更新日: 2024-11-13)

主引用文献

Sun, X.L.,Baker, H.M.,Shewry, S.C.,Jameson, G.B.,Baker, E.N.
Structure of recombinant human lactoferrin expressed in Aspergillus awamori.
Acta Crystallogr.,Sect.D, 55:403-407, 1999

PubMed Abstract: Human lactoferrin (hLf) has considerable potential as a therapeutic agent. Overexpression of hLf in the fungus Aspergillus awamori has resulted in the availability of very large quantities of this protein. Here, the three-dimensional structure of the recombinant hLf has been determined by X-ray crystallography at a resolution of 2.2 A. The final model, comprising 5339 protein atoms (residues 1-691, 294 solvent molecules, two Fe3+and two CO32- ions), gives an R factor of 0.181 (free R = 0.274) after refinement against 32231 reflections in the resolution range 10-2.2 A. Superposition of the recombinant hLf structure onto the native milk hLf structure shows a very high level of correspondence; the main-chain atoms for the entire polypeptide can be superimposed with an r.m.s. deviation of only 0.3 A and there are no significant differences in side-chain conformations or in the iron-binding sites. Dynamic properties, as measured by B-value distributions or iron-release kinetics, also agree closely. This shows that the structure of the protein is not affected by the mode of expression, the use of strain-improvement procedures or the changes in glycosylation due to the fungal system.

PubMed: 10089347
DOI: 10.1107/S0907444998011226

実験手法

X-RAY DIFFRACTION (2.2 Å)