Heteronuclear NMR studies on 44 kDa dimer, syndesmos
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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.
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.
참고문헌 (17)
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