2ran: Difference between revisions
New page: left|200px<br /><applet load="2ran" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ran, resolution 1.89Å" /> '''RAT ANNEXIN V CRYSTA... |
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[[Image:2ran.jpg|left|200px]]<br /><applet load="2ran" size=" | [[Image:2ran.jpg|left|200px]]<br /><applet load="2ran" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ran, resolution 1.89Å" /> | caption="2ran, resolution 1.89Å" /> | ||
'''RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES'''<br /> | '''RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES'''<br /> | ||
==Overview== | ==Overview== | ||
Annexins are a family of calcium- and phospholipid-binding proteins | 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. | ||
==About this Structure== | ==About this Structure== | ||
2RAN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2RAN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RAN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Concha, N | [[Category: Concha, N O.]] | ||
[[Category: Dedman, J | [[Category: Dedman, J R.]] | ||
[[Category: Head, J | [[Category: Head, J F.]] | ||
[[Category: Kaetzel, M | [[Category: Kaetzel, M A.]] | ||
[[Category: Seaton, B | [[Category: Seaton, B A.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: calcium/phospholipid-binding protein]] | [[Category: calcium/phospholipid-binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:46:00 2008'' | ||
Revision as of 16:46, 21 February 2008
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RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES
Overview
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.
About this Structure
2RAN is a Single protein structure of sequence from Rattus norvegicus with CA and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Rat annexin V crystal structure: Ca(2+)-induced conformational changes., Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA, Science. 1993 Sep 3;261(5126):1321-4. PMID:8362244
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