NDLI: Mobility Study of Individual Residue Sites in the Carbohydrate Recognition Domain of LSECtin Using SDSL

Content Provider	Springer Nature Link
Author	Wang, Changzhen Yang, Juntao Zhou, Yu Cong, Jianbo Dong, Guofu Hu, Xiangjun Tang, Li Wu, Ke
Copyright Year	2012
Abstract	Conformational changes in proteins profoundly influence their functional profiles. With site-directed spin labeling (SDSL)–electron paramagnetic resonance (EPR) spectroscopy, we investigated the mobility features of individual residue sites in the carbohydrate recognition domain (CRD) of LSECtin, a type II integral membrane protein. The mobility of six different residue sites scatting around the Ca$^{2+}$-1-binding site were investigated by comparing their EPR spectra rotational correlation time τ $_{c}$ in order to obtain the information of conformational changes of relevant region. The results showed that the overall mobility of LSECtin-CRD increased after addition of Ca$^{2+}$ and N-acetylglucosamine, but different sites in the CRD exhibited different mobility features, suggesting that these sites may have different functional profiles. The preliminary observations thus demonstrated that SDSL–EPR spectroscopy is not only an effective technique to reveal the mobility of single residue sites in LSECtin-CRD but also that the functions of single residue sites may be indicated by their conformational dynamics.
Starting Page	2295
Ending Page	2304
Page Count	10
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	167
Issue Number	8
e-ISSN	15590291
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-06-19
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	SDSL–EPR spectroscopy LSECtin-CRD Cysteine Mobility Biochemistry Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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