Abstract:
:Small-angle X-ray scattering was used to investigate a complex state of apocalmodulin induced by the binding of a Ca(2+)/calmodulin-dependent protein kinase IV calmodulin target site. Upon binding of the peptide, the molecular weight for apocalmodulin increased by 8.4%, which provides direct evidence for the formation of a calmodulin/target peptide complex. Comparison of the radius of gyration and Kratky plots of the apocalmodulin/peptide complex with those of apocalmodulin indicates that the overall conformation remains unchanged but the flexibility of the central linker decreases. An analysis of residue pairs between calmodulin and the target peptides suggests that the complex formation is induced by electrostatic interactions and subsequent van der Waals interactions.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Izumi Y,Kuwamoto S,Jinbo Y,Yoshino Hdoi
10.1016/s0014-5793(01)02375-4keywords:
subject
Has Abstractpub_date
2001-04-20 00:00:00pages
126-30issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02375-4journal_volume
495pub_type
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