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Homology modelling and 1H NMR studies of human leukaemia inhibitory factor.
- Source :
-
FEBS letters [FEBS Lett] 1994 Aug 22; Vol. 350 (2-3), pp. 275-80. - Publication Year :
- 1994
-
Abstract
- Human leukaemia inhibitory factor (LIF) is a glycoprotein with a diverse range of activities on many cell types. A molecular model of LIF has been constructed based mainly on the structure of the related cytokine granulocyte colony-stimulating factor, and refined using simulated annealing and molecular dynamics in water. The model was stable during molecular dynamics refinement and is consistent with known stereochemical data on proteins. It has been assessed by comparison with 1H NMR data on the ionization behaviour of the six histidine residues in LIF, the imidazolium pKa values of which range from 3.6 to 7.4. These pKa values were assigned to individual histidine residues from NMR studies on a series of His-->Ala mutants. The environments of the histidine residues in the model account very well for their observed ionization behaviour. Furthermore, the model is consistent with mutagenesis studies which have defined a group of amino acid residues involved in receptor binding.
- Subjects :
- Amino Acid Sequence
Granulocyte Colony-Stimulating Factor chemistry
Histidine chemistry
Humans
Hydrogen-Ion Concentration
Leukemia Inhibitory Factor
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Sequence Alignment
Sequence Homology, Amino Acid
Stereoisomerism
Growth Inhibitors chemistry
Interleukin-6
Lymphokines chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 350
- Issue :
- 2-3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 7520873
- Full Text :
- https://doi.org/10.1016/0014-5793(94)00785-3