1hse

File:1hse.gif

spinqualitylabelsall models 1hse, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

H253M N TERMINAL LOBE OF HUMAN LACTOFERRIN

Overview

The contribution of the conserved His ligand to iron binding in, transferrins has been addressed by site-directed mutagenesis and X-ray, crystallographic analysis. His 253 in the N-terminal half-molecule of, human lactoferrin, LfN (residues 1-333), has been changed to Gly, Ala, Pro, Thr, Leu, Phe, Met, Tyr, Glu, Gln, and Cys by, oligonucleotide-directed mutagenesis. The proteins have been expressed in, baby hamster kidney cells, at high levels, and purified. The results show, that the His ligand is essential for the stability of the iron binding, site. All of the substitutions destabilized iron binding irrespective of, whether the replacements were potential iron ligands or not. Iron was lost, below pH approximately 6 for the Cys, Glu, and Tyr mutants and below pH 7, or higher for the ... [(full description)]

About this Structure

1HSE is a [Single protein] structure of sequence from [Homo sapiens] with FE and CO3 as [ligands]. Structure known Active Site: S1. Full crystallographic information is available from [OCA].

Reference

Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant., Nicholson H, Anderson BF, Bland T, Shewry SC, Tweedie JW, Baker EN, Biochemistry. 1997 Jan 14;36(2):341-6. PMID:9003186

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