دورية أكاديمية
Picosecond to second dynamics reveals a structural transition in Clostridium botulinum NO-sensor triggered by the activator BAY-41-2272.
| العنوان: | Picosecond to second dynamics reveals a structural transition in Clostridium botulinum NO-sensor triggered by the activator BAY-41-2272. |
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| المؤلفون: | Yoo BK; Laboratoire d'Optique et Biosciences, INSERM U696, CNRS UMR 7645, Ecole Polytechnique, 91128 Palaiseau Cedex, France., Lamarre I, Rappaport F, Nioche P, Raman CS, Martin JL, Negrerie M |
| المصدر: | ACS chemical biology [ACS Chem Biol] 2012 Dec 21; Vol. 7 (12), pp. 2046-54. Date of Electronic Publication: 2012 Oct 02. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101282906 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1554-8937 (Electronic) Linking ISSN: 15548929 NLM ISO Abbreviation: ACS Chem Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, D.C. : American Chemical Society, c2006- |
| مواضيع طبية MeSH: | Bacterial Proteins/*metabolism , Clostridium botulinum/*metabolism , Nitric Oxide/*metabolism , Pyrazoles/*pharmacology , Pyridines/*pharmacology, Amino Acid Sequence ; Bacterial Proteins/chemistry ; Guanylate Cyclase/metabolism ; Ligands ; Molecular Sequence Data ; Nitric Oxide/chemistry ; Protein Conformation ; Receptors, Cytoplasmic and Nuclear/metabolism ; Sequence Homology, Amino Acid ; Soluble Guanylyl Cyclase |
| مستخلص: | Soluble guanylate cyclase (sGC) is the mammalian endogenous nitric oxide (NO) receptor that synthesizes cGMP upon NO activation. In synergy with the artificial allosteric effector BAY 41-2272 (a lead compound for drug design in cardiovascular treatment), sGC can also be activated by carbon monoxide (CO), but the structural basis for this synergistic effect are unknown. We recorded in the unusually broad time range from 1 ps to 1 s the dynamics of the interaction of CO binding to full length sGC, to the isolated sGC heme domain β(1)(200) and to the homologous bacterial NO-sensor from Clostridium botulinum. By identifying all phases of CO binding in this full time range and characterizing how these phases are modified by BAY 41-2272, we show that this activator induces the same structural changes in both proteins. This result demonstrates that the BAY 41-2272 binding site resides in the β(1)(200) sGC heme domain and is the same in sGC and in the NO-sensor from Clostridium botulinum. |
| معلومات مُعتمدة: | R01 GM084700 United States GM NIGMS NIH HHS |
| المشرفين على المادة: | 0 (3-(4-Amino-5-cyclopropylpyrimidine-2-yl)-1-(2-fluorobenzyl)-1H-pyrazolo(3,4-b)pyridine) 0 (Bacterial Proteins) 0 (Ligands) 0 (Pyrazoles) 0 (Pyridines) 0 (Receptors, Cytoplasmic and Nuclear) 31C4KY9ESH (Nitric Oxide) EC 4.6.1.2 (Guanylate Cyclase) EC 4.6.1.2 (Soluble Guanylyl Cyclase) |
| تواريخ الأحداث: | Date Created: 20120927 Date Completed: 20130604 Latest Revision: 20161125 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1021/cb3003539 |
| PMID: | 23009307 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1554-8937 |
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| DOI: | 10.1021/cb3003539 |