2ran: Difference between revisions

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[[Image:2ran.jpg|left|200px]]
{{Seed}}
[[Image:2ran.png|left|200px]]


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{{STRUCTURE_2ran|  PDB=2ran  |  SCENE=  }}  
{{STRUCTURE_2ran|  PDB=2ran  |  SCENE=  }}  


'''RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES'''
===RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES===




==Overview==
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Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes.
The line below this paragraph, {{ABSTRACT_PUBMED_8362244}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8362244 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8362244}}


==About this Structure==
==About this Structure==
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[[Category: Seaton, B A.]]
[[Category: Seaton, B A.]]
[[Category: Calcium/phospholipid-binding protein]]
[[Category: Calcium/phospholipid-binding protein]]
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