1aj5
From Proteopedia
(New page: 200px<br /><applet load="1aj5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aj5, resolution 2.30Å" /> '''CALPAIN DOMAIN VI AP...) |
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| - | [[Image:1aj5.gif|left|200px]]<br /><applet load="1aj5" size=" | + | [[Image:1aj5.gif|left|200px]]<br /><applet load="1aj5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1aj5, resolution 2.30Å" /> | caption="1aj5, resolution 2.30Å" /> | ||
'''CALPAIN DOMAIN VI APO'''<br /> | '''CALPAIN DOMAIN VI APO'''<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== | ||
| - | 1AJ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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:// | + | 1AJ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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=1AJ5 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 11:45:03 2008'' |
Revision as of 09:45, 21 February 2008
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CALPAIN DOMAIN VI APO
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
1AJ5 is a Single protein structure of sequence from Rattus norvegicus. 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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