1b0l

From Proteopedia

RECOMBINANT HUMAN DIFERRIC LACTOFERRIN

Overview

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.

Disease

Known disease associated with this structure: Deafness, autosomal dominant 1 OMIM:[602121]

About this Structure

1B0L is a Single protein structure of sequence from Homo sapiens with FE and CO3 as ligands. Full crystallographic information is available from OCA.

Reference

Structure of recombinant human lactoferrin expressed in Aspergillus awamori., Sun XL, Baker HM, Shewry SC, Jameson GB, Baker EN, Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):403-7. PMID:10089347

Page seeded by OCA on Mon Nov 12 16:04:32 2007