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Title
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Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy.
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Authors
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D.S.Garrett,
P.J.Lodi,
Y.Shamoo,
K.R.Williams,
G.M.Clore,
A.M.Gronenborn.
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Ref.
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Biochemistry, 1994,
33,
2852-2858.
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PubMed id
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Abstract
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The secondary structure and folding topology of the first RNA binding domain of
the human hnRNP A1 protein was determined by multidimensional heteronuclear NMR
spectroscopy. The 92 amino acid long domain exhibits a beta alpha beta beta
alpha beta folding pattern, arranged in a four-stranded antiparallel beta-sheet
flanked by two alpha-helices, which is very similar to that found for other
members of this family. Regions of marked variation between the structurally
characterized RNA binding proteins of this class to date are mainly localized in
the loops connecting the secondary structure elements.
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