Crystal Structure of the T4 regA Translational Regulator Protein at 1.9 Å Resolution-Reference-Cited by-同舟云学术

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Crystal Structure of the T4 regA Translational Regulator Protein at 1.9 Å Resolution

Published:1995-05-26 Issue:5214 Volume:268 Page:1170-1173
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Kang ChulHee¹,Chan Rodney¹,Berger Imre¹²,Lockshin Curtis¹,Green Louis³,Gold Larry⁴,Rich Alexander¹

Affiliation:

1. Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

2. Department of Biophysical Chemistry, Hannover Medical School, 30623 Hannover, Germany.

3. Nexagen Inc., Boulder, CO 80302, USA.

4. Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO 80302, USA.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference21 articles.

1. The 2.9 Å Crystal Structure of T. thermophilus Seryl-tRNA Synthetase Complexed with tRNA Ser

2. X-PLOR

3. Conserved Structures and Diversity of Functions of RNA-Binding Proteins

4. Cavarelli, J., Nature 362:181 (1993).

5. Jones, T. A., Computational Crystallography: 303 (1982).

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1. Post-transcriptional control by bacteriophage T4: mRNA decay and inhibition of translation initiation;Virology Journal;2010-12

2. In vitro selection of phage RB69 RegA RNA binding sites yields UAA triplets;Virology;2005-05

3. Overview of Protein Structural and Functional Folds;Current Protocols in Protein Science;2004-02

4. References;RNA Motifs and Regulatory Elements;2002

5. RegA proteins from phage T4 and RB69 have conserved helix-loop groove RNA binding motifs but different RNA binding specificities;Nucleic Acids Research;2001-03-01

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