Abstract
Crystal structures of unbound protein L1 and of its complexes with ribosomal an messenger RNAs are analyzed. It is shown that the values of the apparent association rate constant for L1-RNA depend on conformation of unbound protein L1. It is suggested that L1 binds to rRNA with higher affinity than to mRNA because of additional interactions between domain II of L1 and the loop rRNA region, which is absent in mRNA.
Publication types
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English Abstract
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Archaeal Proteins / metabolism
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Bacterial Proteins / metabolism
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Models, Molecular
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Protein Binding
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Protein Biosynthesis
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Protein Conformation
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RNA, Archaeal / metabolism
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RNA, Bacterial / metabolism
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RNA, Messenger / metabolism*
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RNA, Ribosomal / metabolism*
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Ribosomal Proteins / metabolism*
Substances
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Archaeal Proteins
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Bacterial Proteins
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RNA, Archaeal
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RNA, Bacterial
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RNA, Messenger
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RNA, Ribosomal
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Ribosomal Proteins
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ribosomal protein L1