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| 024 | 7 | _ | |2 pmid |a pmid:21430265 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC3076860 |
| 024 | 7 | _ | |2 DOI |a 10.1073/pnas.1015890108 |
| 024 | 7 | _ | |2 WOS |a WOS:000289413600042 |
| 037 | _ | _ | |a PreJuSER-16576 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 000 |
| 084 | _ | _ | |2 WoS |a Multidisciplinary Sciences |
| 100 | 1 | _ | |a Schünke, S. |b 0 |u FZJ |0 P:(DE-Juel1)VDB72730 |
| 245 | _ | _ | |a Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel |
| 260 | _ | _ | |a Washington, DC |b Academy |c 2011 |
| 300 | _ | _ | |a 6121 - 6126 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |a Proceedings of the National Academy of Sciences of the United States of America |x 0027-8424 |0 5100 |y 15 |v 108 |
| 500 | _ | _ | |a This study was supported by a fellowship from the International Research School BioStruct to S.S. and a research grant from the Helmholtz-Gemeinschaft (Virtual Institute of Structural Biology) to D.W. |
| 520 | _ | _ | |a Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are activated by binding of ligands to a domain (CNBD) located on the cytoplasmic side of the channel. The underlying mechanisms are not well understood. To elucidate the gating mechanism, structures of both the ligand-free and -bound CNBD are required. Several crystal structures of the CNBD from HCN2 and a bacterial CNG channel (MloK1) have been solved. However, for HCN2, the cAMP-free and -bound state did not reveal substantial structural rearrangements. For MloK1, structural information for the cAMP-free state has only been gained from mutant CNBDs. Moreover, in the crystal, the CNBD molecules form an interface between dimers, proposed to be important for allosteric channel gating. Here, we have determined the solution structure by NMR spectroscopy of the cAMP-free wild-type CNBD of MloK1. A comparison of the solution structure of cAMP-free and -bound states reveals large conformational rearrangement on ligand binding. The two structures provide insights on a unique set of conformational events that accompany gating within the ligand-binding site. |
| 536 | _ | _ | |a Funktion und Dysfunktion des Nervensystems |c P33 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK409 |x 0 |
| 536 | _ | _ | |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |0 G:(DE-Juel1)FUEK505 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Alphaproteobacteria: metabolism |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Cyclic AMP: chemistry |
| 650 | _ | 2 | |2 MeSH |a Cyclic Nucleotide-Gated Cation Channels: chemistry |
| 650 | _ | 2 | |2 MeSH |a Cyclic Nucleotide-Gated Cation Channels: genetics |
| 650 | _ | 2 | |2 MeSH |a Mutation |
| 650 | _ | 2 | |2 MeSH |a Nuclear Magnetic Resonance, Biomolecular |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Cyclic Nucleotide-Gated Cation Channels |
| 650 | _ | 7 | |0 60-92-4 |2 NLM Chemicals |a Cyclic AMP |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a NMR solution structure |
| 653 | 2 | 0 | |2 Author |a apo state |
| 653 | 2 | 0 | |2 Author |a ligand removal method |
| 653 | 2 | 0 | |2 Author |a potassium channel |
| 700 | 1 | _ | |a Stoldt, M. |b 1 |u FZJ |0 P:(DE-Juel1)VDB21601 |
| 700 | 1 | _ | |a Lecher, J. |b 2 |u FZJ |0 P:(DE-Juel1)VDB94799 |
| 700 | 1 | _ | |a Kaupp, U.B. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Willbold, D. |b 4 |u FZJ |0 P:(DE-Juel1)132029 |
| 773 | _ | _ | |a 10.1073/pnas.1015890108 |g Vol. 108, p. 6121 - 6126 |p 6121 - 6126 |q 108<6121 - 6126 |0 PERI:(DE-600)1461794-8 |t Proceedings of the National Academy of Sciences of the United States of America |v 108 |y 2011 |x 0027-8424 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3076860 |
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| 914 | 1 | _ | |y 2011 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
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