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Crystallization and preliminary X‐ray analysis of leukemia inhibitory factor
Author(s) -
Betzel Christian,
Visanji Marcia,
Dauter Zbigniew,
Fourme Roger,
Weber Wolfgang,
Marnitz Ulf,
Boone Thomas,
Pope Joseph,
Miller James,
Hawkins Nessa,
Samal Babru
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80810-h
Subject(s) - leukemia inhibitory factor , oncostatin m , leukemia inhibitory factor receptor , glycoprotein 130 , chemistry , ciliary neurotrophic factor , in vitro , glycosylation , glycoprotein , interleukin 6 , microbiology and biotechnology , biology , biochemistry , receptor , cytokine , immunology , neurotrophic factors
Leukemia inhibitory factor (LIF) is a polyfunctional molecule with significant and diverse biological activities. LIF is a glycoprotein secreted by a number of different cell types in vitro. It is induced in fibroblasts, lymphocytes, monocytes and astrocytes by various inducers such as serum, TNF, interleukin‐IP and EGF. Due to extensive and variable glycosylation the molecular weight can range from 38 to 67 kDA. The biological functions of LIF are mediated through a receptor and a signal transducer, gp130, which is also used by factors like interleukm‐6 (IL‐6), cilliary neurotropic factor (CNTF), and oncostatin M (OSM). Here, we report the crystallization of the non‐glycosylated human‐like LIF expressed in E. coli . The present crystals diffract to 2.0 Å using synchrotron radiation. They belong to the monoclinic space group C2, and the cell dimensions are a = 61.5 Å, b = 45.3 Å , c =77.7 Å and β = 112.3°.