1avc: Difference between revisions

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New page: left|200px<br /><applet load="1avc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avc, resolution 2.90Å" /> '''BOVINE ANNEXIN VI (C...
 
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[[Image:1avc.gif|left|200px]]<br /><applet load="1avc" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1avc.gif|left|200px]]<br /><applet load="1avc" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1avc, resolution 2.90&Aring;" />
caption="1avc, resolution 2.90&Aring;" />
'''BOVINE ANNEXIN VI (CALCIUM-BOUND)'''<br />
'''BOVINE ANNEXIN VI (CALCIUM-BOUND)'''<br />


==Overview==
==Overview==
The crystal structure of a calcium-bound form of bovine annexin VI has, been determined with X-ray diffraction data to 2.9 A by molecular, replacement. Six Ca2+ ions were found, five in AB loops, one in a DE loop., Two loops (II-AB, which binds calcium, and V-AB, which does not) have, conformations that differ significantly from those in calcium-free, human, recombinant annexin VI. There are only small differences between the, calci- and the apo-annexin VI in the rest of the molecule. Calcium by, itself does not promote a major conformational change.
The crystal structure of a calcium-bound form of bovine annexin VI has been determined with X-ray diffraction data to 2.9 A by molecular replacement. Six Ca2+ ions were found, five in AB loops, one in a DE loop. Two loops (II-AB, which binds calcium, and V-AB, which does not) have conformations that differ significantly from those in calcium-free, human recombinant annexin VI. There are only small differences between the calci- and the apo-annexin VI in the rest of the molecule. Calcium by itself does not promote a major conformational change.


==About this Structure==
==About this Structure==
1AVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AVC OCA].  
1AVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVC OCA].  


==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Avila-Sakar, A.J.]]
[[Category: Avila-Sakar, A J.]]
[[Category: Creutz, C.E.]]
[[Category: Creutz, C E.]]
[[Category: Kretsinger, R.H.]]
[[Category: Kretsinger, R H.]]
[[Category: CA]]
[[Category: CA]]
[[Category: annexin]]
[[Category: annexin]]
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[[Category: membrane-binding]]
[[Category: membrane-binding]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:09:19 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:39 2008''

Revision as of 12:48, 21 February 2008

File:1avc.gif


1avc, resolution 2.90Å

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BOVINE ANNEXIN VI (CALCIUM-BOUND)

OverviewOverview

The crystal structure of a calcium-bound form of bovine annexin VI has been determined with X-ray diffraction data to 2.9 A by molecular replacement. Six Ca2+ ions were found, five in AB loops, one in a DE loop. Two loops (II-AB, which binds calcium, and V-AB, which does not) have conformations that differ significantly from those in calcium-free, human recombinant annexin VI. There are only small differences between the calci- and the apo-annexin VI in the rest of the molecule. Calcium by itself does not promote a major conformational change.

About this StructureAbout this Structure

1AVC is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of bovine annexin VI in a calcium-bound state., Avila-Sakar AJ, Creutz CE, Kretsinger RH, Biochim Biophys Acta. 1998 Sep 8;1387(1-2):103-16. PMID:9748523

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