1dvi
From Proteopedia
(New page: 200px<br /><applet load="1dvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dvi, resolution 2.30Å" /> '''CALPAIN DOMAIN VI WI...) |
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| - | [[Image:1dvi.gif|left|200px]]<br /><applet load="1dvi" size=" | + | [[Image:1dvi.gif|left|200px]]<br /><applet load="1dvi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dvi, resolution 2.30Å" /> | caption="1dvi, resolution 2.30Å" /> | ||
'''CALPAIN DOMAIN VI WITH CALCIUM BOUND'''<br /> | '''CALPAIN DOMAIN VI WITH CALCIUM BOUND'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a Ca(2+)-binding domain (dVI) of rat m-calpain | + | The crystal structure of a Ca(2+)-binding domain (dVI) of rat m-calpain has been determined at 2.3 A resolution, both with and without bound Ca2+. The structures reveal a unique fold incorporating five EF-hand motifs per monomer, three of which bind calcium at physiological calcium concentrations, with one showing a novel EF-hand coordination pattern. This investigation gives us a first view of the calcium-induced conformational changes, and consequently an insight into the mechanism of calcium induced activation in calpain. The crystal structures reveal a dVI homodimer which provides a preliminary model for the subunit dimerization in calpain. |
==About this Structure== | ==About this Structure== | ||
| - | 1DVI 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 and 3.4.22.53 3.4.22.52 and 3.4.22.53] Full crystallographic information is available from [http:// | + | 1DVI 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 and 3.4.22.53 3.4.22.52 and 3.4.22.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: small subunit]] | [[Category: small subunit]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:56 2008'' |
Revision as of 10:21, 21 February 2008
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CALPAIN DOMAIN VI WITH CALCIUM BOUND
Overview
The crystal structure of a Ca(2+)-binding domain (dVI) of rat m-calpain has been determined at 2.3 A resolution, both with and without bound Ca2+. The structures reveal a unique fold incorporating five EF-hand motifs per monomer, three of which bind calcium at physiological calcium concentrations, with one showing a novel EF-hand coordination pattern. This investigation gives us a first view of the calcium-induced conformational changes, and consequently an insight into the mechanism of calcium induced activation in calpain. The crystal structures reveal a dVI homodimer which provides a preliminary model for the subunit dimerization in calpain.
About this Structure
1DVI is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53 Full crystallographic information is available from OCA.
Reference
Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes., Blanchard H, Grochulski P, Li Y, Arthur JS, Davies PL, Elce JS, Cygler M, Nat Struct Biol. 1997 Jul;4(7):532-8. PMID:9228945
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