1anw

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[[Image:1anw.gif|left|200px]]
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{{STRUCTURE_1anw| PDB=1anw | SCENE= }}
{{STRUCTURE_1anw| PDB=1anw | SCENE= }}
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'''THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING'''
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===THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 1446685 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1446685}}
==About this Structure==
==About this Structure==
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[[Category: Morera, S.]]
[[Category: Morera, S.]]
[[Category: Calcium/phospholipid-binding protein]]
[[Category: Calcium/phospholipid-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:29:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:14:14 2008''

Revision as of 14:14, 30 June 2008

Image:1anw.png

Template:STRUCTURE 1anw

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

Template:ABSTRACT PUBMED 1446685

About this Structure

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

Reference

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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