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Title
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1H, 13C, and 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins.
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Authors
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M.Wittekind,
M.Görlach,
M.Friedrichs,
G.Dreyfuss,
L.Mueller.
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Ref.
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Biochemistry, 1992,
31,
6254-6265.
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PubMed id
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Abstract
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The hnRNP C1 and C2 proteins are abundant nuclear proteins that bind avidly to
heterogeneous nuclear RNAs (hnRNAs) and appear to be involved with pre-mRNA
processing. The RNA-binding activity of the hnRNP C proteins is contained in the
amino-terminal 94 amino acid RNA-binding domain (RBD) that is identical for
these two proteins. We have obtained the 1H, 13C, and 15N NMR assignments for
the RBD of the human hnRNP C proteins. The assignment process was facilitated by
extensive utilization of three- and four-dimensional heteronuclear-edited
spectra. Sequential assignments of the backbone resonances were made using a
combination of 15N-edited 3D NOESY-HMQC, 3D TOCSY-HMQC, and 3D TOCSY-NOESY-HSQC
as well as 3D HNCA, HNCO, and HCACO spectra. Side-chain resonances were assigned
using 3D HCCH-COSY and 3D HCH-TOCSY spectra. Four-dimensional 13C/13C-edited
NOESY and 13C/15N-edited NOESY experiments were used to unambigously resolve
NOEs. The overall global folding pattern was established by calculating a set of
preliminary structures using constraints derived from the sequential NOEs and a
small number of long-range NOEs. The beta alpha beta-beta alpha beta domain
structure exhibits an antiparallel beta-sheet with the conserved RNP 1 and RNP 2
sequences [Dreyfuss et al. (1988) Trends Biochem. Sci. 13, 86-91] located
adjacent to one another as the two inner strands of the beta-sheet.
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