Calponin binds G-actin and F-actin with similar affinity
| Autor: | Sutherland K. Maciver, Claude Roustan, Abdellatif Fattoum, Yves Benyamin, Mohamed Manai, Imen Ferjani |
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| Rok vydání: | 2006 |
| Předmět: |
Cell signaling
Calponin Biophysics Muscle Proteins macromolecular substances Calponin homology domain Biochemistry Filamentous actin Structural Biology Genetics Animals Cysteine Cytoskeleton Molecular Biology Actin Protein kinase C Fluorescent Dyes Binding Sites biology Calcium-Binding Proteins Microfilament Proteins Muscle Smooth Cell Biology musculoskeletal system Fluorescence Actins Cell biology Spectrometry Fluorescence biology.protein Rabbits Protein Binding Cell signalling |
| Zdroj: | FEBS Letters. 580:4801-4806 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2006.07.065 |
| Popis: | Calponins are actin-binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F-actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle calponin binds monomeric actin with a similar affinity ( K d of 0.15 μM). We show that the arrangement of binding is similar to that of F-actin by a number of criteria, most notably that the distance between Cys273 on calponin and Cys374 of actin is 29 A when measured by fluorescent resonance energy transfer, the same distance as previously reported for F-actin. |
| Databáze: | OpenAIRE |
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