Increase in the molecular weight and radius of gyration of apocalmodulin induced by binding of target peptide: evidence for complex formation.

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 Lett

journal_title

FEBS letters

authors

Izumi Y,Kuwamoto S,Jinbo Y,Yoshino H

doi

10.1016/s0014-5793(01)02375-4

keywords:

subject

Has Abstract

pub_date

2001-04-20 00:00:00

pages

126-30

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02375-4

journal_volume

495

pub_type

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