JKMRS Volume 19, No 2, pp 83-87;Heteronuclear NMR studies on 4... | |
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2015년 10월 13일 / 조회수: 632 | |
Heteronuclear
NMR studies on 44 kDa dimer, syndesmos Heeyoun Kim1, Inhwan Lee1, Jeongmin
Han1, Hae-kap Cheong2 , Eunhee Kim2 and
Weontae Lee*1 1Department of Biochemistry,
College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea 2Magnetic Resonance Team,Korea
Basic Science Institute (KBSI), Ochang, Chungbuk 363-883, Korea Received July 29, 2015; Revised
Aug 21, 2015; Accepted Sep 10, 2015 Abstract Syndesmos, which is
co-localized with syndecan-4 cytoplasmic domain (Syn4cyto) in focal contacts,
interacts with various cell adhesion adaptor proteins including Syn4cyto to
control cell signaling. Syndesmos consists of 211 amino acids and it exists as
a dimer (44kDa) in solution. Recently, we have determined the structure of syndesmos
by x-ray crystallography, however, dynamics related to syndecan binding still
remain elusive. In this report, we performed NMR experiments to acquire
biochemical and structural information of syndesmos. Based on a series of
three-dimensional triple resonance experiments on a 13C/15N/2H
labeled protein, NMR spectra were obtained with well dispersed and homogeneous
NMR data. We present the sequence specific backbone assignment of syndesmos and
assigned NMR data with combination structural information can be directly used
for the studies on interaction with Syn4cyto and other binding molecules. |
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첨부파일 | 5_이원태.pdf |