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Biophysical Journal 71: 1920-1933 (1996)
© 1996 the Biophysical Society

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Affinity and structure of complexes of tropomyosin and caldesmon domains.

E J Hnath, C L Wang, P A Huber, S B Marston and G N Phillips, Jr

Department of Biochemistry and Cell Biology, W.M. Keck Center for Computational Biology, Rice University, Houston, Texas 77005, USA.

ABSTRACT

The interaction of caldesmon domains with tropomyosin has been studied using x-ray crystallography and an optical biosensor. Only whole caldesmon and the carboxyl-terminal domain of caldesmon (CaD-4, chicken gizzard residues 597-756) bound to tropomyosin with greater than millimolar affinity at 100 and 150 microM salt. Under these conditions the affinities of whole caldesmon and CaD-4 were both in the micromolar range. Data from the x-ray studies showed that whole caldesmon bound to tropomyosin in several places, with the region of tightest interaction being at tropomyosin residues 70-100 and/or 230-260. Studies with CaD-4 revealed that this region corresponded to the strong binding site seen with whole caldesmon. Weaker association of other regions of caldesmon to tropomyosin residues 180-210 and 5-50 was also observed. The results suggest that the carboxyl-terminus of caldesmon binds tightly to tropomyosin and that other regions of caldesmon may interact with tropomyosin tightly only when they are held close to tropomyosin by the carboxyl-terminal domain. Four models are presented to show the possible interactions of caldesmon with tropomyosin.




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Copyright © 1996 by the Biophysical Society.