1anw

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THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING

File:1anw.gif


1anw, resolution 2.40Å

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OverviewOverview

The structure of annexin V, crystallised in the presence of two calcium or, barium ions for each protein molecule, was solved by molecular replacement, to 0.24 nm resolution. The two metal ions are found in domains I and IV, i.e. on the same side of the channel that lies in the centre of the, molecule. The structures of the barium and calcium form are extremely, close, the only differences localised in the metal-binding sites that lie, on the surface of the molecule. The occupancies of the metal ions, however, are lower for barium than for calcium, expressing the lower, affinity of the protein for the former. The packing of the annexin, molecules in the crystal asymmetric unit may represent a model for the, calcium driven association of membrane-bound annexins that leads to, membrane fusion.

About this StructureAbout this Structure

1ANW is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.

ReferenceReference

The effect of metal binding on the structure of annexin V and implications for membrane binding., Lewit-Bentley A, Morera S, Huber R, Bodo G, Eur J Biochem. 1992 Nov 15;210(1):73-7. PMID:1446685

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