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PDBsum entry 2up1
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Gene regulation/DNA
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PDB id
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2up1
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the two-Rrm domain of hnrnp a1 (up1) complexed with single-Stranded telomeric DNA.
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Authors
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J.Ding,
M.K.Hayashi,
Y.Zhang,
L.Manche,
A.R.Krainer,
R.M.Xu.
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Ref.
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Genes Dev, 1999,
13,
1102-1115.
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PubMed id
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Abstract
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Human hnRNP A1 is a versatile single-stranded nucleic acid-binding protein that
functions in various aspects of mRNA maturation and in telomere length
regulation. The crystal structure of UP1, the amino-terminal domain of human
hnRNP A1 containing two RNA-recognition motifs (RRMs), bound to a 12-nucleotide
single-stranded telomeric DNA has been determined at 2.1 A resolution. The
structure of the complex reveals the basis for sequence-specific recognition of
the single-stranded overhangs of human telomeres by hnRNP A1. It also provides
insights into the basis for high-affinity binding of hnRNP A1 to certain RNA
sequences, and for nucleic acid binding and functional synergy between the RRMs.
In the crystal structure, a UP1 dimer binds to two strands of DNA, and each
strand contacts RRM1 of one monomer and RRM2 of the other. The two DNA strands
are antiparallel, and regions of the protein flanking each RRM make important
contacts with DNA. The extensive protein-protein interface seen in the crystal
structure of the protein-DNA complex and the evolutionary conservation of the
interface residues suggest the importance of specific protein-protein
interactions for the sequence-specific recognition of single-stranded nucleic
acids. Models for regular packaging of telomere 3' overhangs and for
juxtaposition of alternative 5' splice sites are proposed.
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