Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1804, Issue 11, Pages 2102-2110Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2010.07.020
Keywords
Lipocalin 12 (Lcn12); Epididymis; beta-Barrel; Cysteine; Disulfide bond; Retinoic acid
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Funding
- Natural Science Foundation of China [30730026]
- Chinese Academy of Sciences (CAS) [KSCX1-YW-R-54, KSCX2-YW-R-104]
- National Science & Technology Major ProjectKey New Drug Creation and Manufacturing Program, China [2009ZX09301-001]
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Lipocalin 12 (Lcn12) is a recently identified epididymis-specific protein that might play a significant physiological role in male reproduction. However, the detailed structure and function of Lcn12 remain to be determined. In the present work, we cloned, expressed, and purified the rat Lcn12 (rLcn12) protein in Escherichia coli, introduced the Cys176Ala substitution to eliminate the aggregation problem associated with the wild-type protein. Homology modeling results demonstrated that rLcn12 adopted an eight-stranded, antiparallel beta-barrel conformation containing a conserved disulfide bond between Cys98 and Cys203, which was in accordance with the physicochemical properties elucidated by a combination of mass, circular dichroism, and nuclear magnetic resonance spectrometry. The purified rLcn12 protein exhibited a high binding affinity for all-trans retinoic acid in fluorescence titration experiments, implying that rLcn12 could be involved in retinoic acid transport in the epididymis. (C) 2010 Elsevier B.V. All rights reserved.
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