Abstract
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
Å when measured by fluorescent resonance energy transfer, the same distance as previously reported for F-actin.