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Title
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1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin.
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Authors
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M.Baron,
A.L.Main,
P.C.Driscoll,
H.J.Mardon,
J.Boyd,
I.D.Campbell.
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Ref.
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Biochemistry, 1992,
31,
2068-2073.
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PubMed id
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Abstract
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The secondary structure of the tenth type III module from human fibronectin has
been determined using NMR. This type of module appears many times in a wide
variety of proteins. The type III module described here contains an Arg-Gly-Asp
sequence known to be involved in cell-cell adhesion. The module was expressed in
yeast and characterized by amino acid sequencing and mass spectrometry. 2D and
3D NMR spectroscopy of 15N-labeled protein was used to perform sequence-specific
assignment of the spectrum. The secondary structure was defined by patterns of
nuclear Overhauser effects, 3JNH-alpha CH spin-spin coupling constants, and
amide proton solvent exchange rates. The molecule consists of seven beta-strands
in two antiparallel beta-sheets with an immunoglobulin-like fold similar to that
predicted for homologous modules in the cytokine receptor super family [Bazan,
J. F. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 6934-6938]. The Arg-Gly-Asp
sequence is located on a loop between the beta-strands F and G.
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