1anw: Difference between revisions
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[[Image:1anw.gif|left|200px]] | [[Image:1anw.gif|left|200px]] | ||
'''THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING''' | {{Structure | ||
|PDB= 1anw |SIZE=350|CAPTION= <scene name='initialview01'>1anw</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ANW is a [ | 1ANW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANW OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1446685 1446685] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium/phospholipid-binding protein]] | [[Category: calcium/phospholipid-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:05 2008'' | ||
Revision as of 11:00, 20 March 2008
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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
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