2ran: Difference between revisions
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[[Image:2ran.jpg|left|200px]] | [[Image:2ran.jpg|left|200px]] | ||
'''RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES''' | {{Structure | ||
|PDB= 2ran |SIZE=350|CAPTION= <scene name='initialview01'>2ran</scene>, resolution 1.89Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2RAN is a [ | 2RAN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RAN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8362244 8362244] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium/phospholipid-binding protein]] | [[Category: calcium/phospholipid-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:34:11 2008'' | ||
Revision as of 16:34, 20 March 2008
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| 2ran, resolution 1.89Å | |||||||||||||
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| Ligands: | CA and SO4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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