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Title
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The crystal structure of annexin VI indicates relative rotation of the two lobes upon membrane binding.
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Authors
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H.Kawasaki,
A.Avila-Sakar,
C.E.Creutz,
R.H.Kretsinger.
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Ref.
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Biochim Biophys Acta, 1996,
1313,
277-282.
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PubMed id
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Abstract
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The crystal structure of bovine liver annexin VI has been determined to low
resolution by molecular replacement. The first lobe (domains 1-4) is rotated
about 90 degrees relative to the second lobe (domains 5-8). Since the same
crystal form (P4(3), 68 X 68 X 205 A) grew from (NH4)2SO4, polyethylene glycol,
and sodium acetate with and without added calcium, this probably reflects the
structure in solution. When bound to a lipid monolayer both lobes of annexin VI
are coplanar. This implies a significant change in conformation upon binding to
membranes.
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