Conformational change in thrombospondin induced by removal of bound Ca2+. A spin label approach.

Abstract:

:The effect of removal of Ca2+ bound to thrombospondin (TSP) on the protein structure in solution has been investigated using ESR spin-label techniques. A maleimide spin label was selectively attached to the free thiol group presumably near the carboxyl-terminal domain in which Ca2+-binding sites are situated. The ESR spectra of spin-labeled TSP showed that the bound label undergoes a relatively fast rotational motion with an effective rotational correlation time in the nano-second time regimes. Removal of bound Ca2+ in TSP by dialyzing spin-labeled TSP from a Ca2+-containing buffer into an EDTA-containing buffer resulted in an increase in the mobility of the bound label by a factor of 2.3. The data suggest that EDTA chelation of bound Ca2+ in TSP induces a conformational change of TSP at least near the site of spin labeling.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Slane JM,Mosher DF,Lai CS

doi

10.1016/0014-5793(88)81157-8

subject

Has Abstract

pub_date

1988-03-14 00:00:00

pages

363-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(88)81157-8

journal_volume

229

pub_type

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