1avc: Difference between revisions

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[[Image:1avc.gif|left|200px]]
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{{STRUCTURE_1avc|  PDB=1avc  |  SCENE=  }}  
{{STRUCTURE_1avc|  PDB=1avc  |  SCENE=  }}  


'''BOVINE ANNEXIN VI (CALCIUM-BOUND)'''
===BOVINE ANNEXIN VI (CALCIUM-BOUND)===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9748523}}


==About this Structure==
==About this Structure==
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[[Category: Calcium/phospholipid-binding protein]]
[[Category: Calcium/phospholipid-binding protein]]
[[Category: Membrane-binding]]
[[Category: Membrane-binding]]
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Revision as of 17:40, 30 June 2008

File:1avc.png

Template:STRUCTURE 1avc

BOVINE ANNEXIN VI (CALCIUM-BOUND)BOVINE ANNEXIN VI (CALCIUM-BOUND)

Template:ABSTRACT PUBMED 9748523

About this StructureAbout this Structure

1AVC is a Single protein structure of sequence from Bos taurus. 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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