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'''THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING''' | '''THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING''' | ||
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[[Category: Lewit-Bentley, A.]] | [[Category: Lewit-Bentley, A.]] | ||
[[Category: Morera, S.]] | [[Category: Morera, S.]] | ||
[[Category: | [[Category: Calcium/phospholipid-binding protein]] | ||
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Revision as of 10:29, 2 May 2008
THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING
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. 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 Page seeded by OCA on Fri May 2 10:29:33 2008