Skip Navigation


Journal of Biochemistry Advance Access originally published online on December 15, 2007
Journal of Biochemistry 2008 143(2):163-167; doi:10.1093/jb/mvm238
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
143/2/163    most recent
mvm238v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Won, H.-S.
Right arrow Articles by Lee, B.-J.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Won, H.-S.
Right arrow Articles by Lee, B.-J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Japanese Biochemical Society.

Rapid Communication

Interdomain interaction of cyclic AMP receptor protein in the absence of cyclic AMP

Hyung-Sik Won1,*, Min-Duk Seo2, Hyun-Suk Ko1, Wahn Soo Choi3 and Bong-Jin Lee2,{dagger}

1Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk 380-701; 2Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742; and 3Department of Immunology, College of Medicine, Konkuk University, Chungju, Chungbuk 380-701, Korea

*To whom correspondence should be addressed. Tel: +82 43 840 3589, Fax: +82 43 852 3616, E-mail: wonhs{at}kku.ac.kr

{dagger}Correspondence may also be addressed. Tel: +82 2 880 7869, Fax: +82 2 872 3632, E-mail: lbj{at}nmr.snu.ac.kr

Received November 6, 2007; Accepted November 30, 2007


  Abstract

Interdomain interaction of apo-cyclic AMP receptor protein (apo-CRP) was qualified using its isolated domains. The cAMP-binding domain was prepared by a limited proteolysis, while the DNA-binding domain was constructed as a recombinant protein. Three different regions making interdomain contacts in apo-CRP were identified by a sequence-specific comparison of the HSQC spectra. The results indicated that apo-CRP possesses characteristic modules of interdomain interaction that are properly organized to suppress activity and to sense and transfer the cAMP binding signals. Particularly, the inertness of the DNA-binding motif in apo-CRP was attributable to the participation of F-helices in the interdomain contacts.

Key Words: allostery, cyclic AMP receptor protein, heteronuclear single quantum coherence, interdomain interaction, nuclear magnetic resonance

Abbreviations: CRP, cyclic AMP receptor protein; NTD, N-terminal domain; CTD, C-terminal domain; CH{alpha}CRP, dimeric NTD of CRP (residues 1–136) generated by chymotrypsin digestion; βCRPC, dimeric CTD of CRP (residues 110–209) containing the C-helices; HSQC, heteronuclear single quantum coherence


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.