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1lki

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Image:1lki.gif

1lki, resolution 2.0Å

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THE CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTION OF LEUKEMIA INHIBITORY FACTOR: IMPLICATIONS FOR RECEPTOR BINDING

Overview

The structure of murine leukemia inhibitory factor (LIF) has been determined by X-ray crystallography at 2.0 A resolution. The main chain fold conforms to the four alpha-helix bundle topology previously observed for several members of the hematopoietic cytokine family. Of these, LIF shows closest structural homology to granulocyte colony-stimulating factor and growth hormone (GH). Sequence alignments for the functionally related molecules oncostatin M and ciliary neurotrophic factor, when mapped to the LIF structure, indicate regions of conserved surface character. Analysis of the biological function and receptor specificity of a series of human-mouse LIF chimeras implicate two regions of receptor interaction that are located in the fourth helix and the preceding loop. A model for receptor binding based on the structure of the GH ligand-receptor complex requires additional, novel features to account for these data.

About this Structure

1LKI is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding., Robinson RC, Grey LM, Staunton D, Vankelecom H, Vernallis AB, Moreau JF, Stuart DI, Heath JK, Jones EY, Cell. 1994 Jul 1;77(7):1101-16. PMID:8020098

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