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PDBsum entry 1vec
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RNA binding protein
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PDB id
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1vec
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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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Structural insight of human dead-Box protein rck/p54 into its substrate recognition with conformational changes.
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Authors
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T.Matsui,
K.Hogetsu,
J.Usukura,
T.Sato,
T.Kumasaka,
Y.Akao,
N.Tanaka.
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Ref.
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Genes Cells, 2006,
11,
439-452.
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PubMed id
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Abstract
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Human rck/p54, a product of the gene cloned at the breakpoint of t(11; 14)
(q23;q32) chromosomal translocation on 11q23 in B-cell lymphoma, is a member of
the DEAD-box RNA helicase family. Here, the crystal structure of Nc-rck/p54, the
N-terminal core domain of rck/p54, revealed that the P-loop in motif I formed a
closed conformation, which was induced by Asn131, a residue unique to the RCK
subfamily. It appears that ATP does not bind to the P-loop. The results of
dynamic light scattering revealed to ATP-induced conformational change of
rck/p54. It was demonstrated that free rck/p54 is a distended molecule in
solution, and that the approach between N-terminal core and C-terminal domains
for ATP binding would be essential when unwinding RNA. The results from helicase
assay using electron micrograph, ATP hydrolytic and luciferase assay showed that
c-myc IRES RNA, whose secondary structure regulates IRES-dependant translation,
was unwound by rck/p54 and indicated that it is a good substrate for rck/p54.
Over-expression of rck/p54 in HeLa cells caused growth inhibition and cell cycle
arrest at G2/M with down-regulation of c-myc expression. These findings
altogether suggest that rck/p54 may affect the IRES-dependent translation of
c-myc even in the cells.
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