2ran
From Proteopedia
(New page: 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 and 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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