Literature DB >> 12153712

Solution structure of a SRP19 binding domain in human SRP RNA.

Taiichi Sakamoto1, Satoshi Morita, Kazutoshi Tabata, Kouji Nakamura, Gota Kawai.   

Abstract

Assembly of the human signal recognition particle (SRP) requires SRP19 protein to bind to helices 6 and 8 of SRP RNA. In the present study, structure of a 29-mer RNA composing the SRP19 binding site in helix 6 was determined by NMR spectroscopy. The two A:C mismatches were continuously stacked to each other and formed wobble type A:C base pairs. The GGAG tetraloop in helix 6 was found to adopt a similar conformation to that of GNRA tetraloop, suggesting that these tetraloops are included in an extensive new motif GNRR. Compared with the crystal structure of helix 6 in complex with SRP19 determined previously, the GGAG tetraloop in the complex was found to adopt a similar conformation to the free form, although the loop structure becomes more open upon SRP19 binding. Thus, SRP19 is thought to recognize the overall fold of the GGAG loop.

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Year:  2002        PMID: 12153712     DOI: 10.1093/oxfordjournals.jbchem.a003207

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  5 in total

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Journal:  RNA       Date:  2009-09-09       Impact factor: 4.942

2.  Analysis of stacking overlap in nucleic acid structures: algorithm and application.

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Journal:  J Comput Aided Mol Des       Date:  2014-07-03       Impact factor: 3.686

3.  Solution structure of an RNA stem-loop derived from the 3' conserved region of eel LINE UnaL2.

Authors:  Seiki Baba; Masaki Kajikawa; Norihiro Okada; Gota Kawai
Journal:  RNA       Date:  2004-07-23       Impact factor: 4.942

4.  Transposable elements in disease-associated cryptic exons.

Authors:  Igor Vorechovsky
Journal:  Hum Genet       Date:  2009-10-10       Impact factor: 4.132

5.  Fifty years of Protein Data Bank in the Journal of Biochemistry.

Authors:  Genji Kurisu
Journal:  J Biochem       Date:  2022-01-07       Impact factor: 3.387

  5 in total

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