1kxr
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1kxr.gif|left|200px]] | + | [[Image:1kxr.gif|left|200px]] |
| - | + | ||
| - | '''Crystal Structure of Calcium-Bound Protease Core of Calpain I''' | + | {{Structure |
| + | |PDB= 1kxr |SIZE=350|CAPTION= <scene name='initialview01'>1kxr</scene>, resolution 2.07Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= CAPN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Calcium-Bound Protease Core of Calpain I''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1KXR is a [ | + | 1KXR 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=1KXR OCA]. |
==Reference== | ==Reference== | ||
| - | A Ca(2+) switch aligns the active site of calpain., Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL, Cell. 2002 Mar 8;108(5):649-60. PMID:[http:// | + | A Ca(2+) switch aligns the active site of calpain., Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL, Cell. 2002 Mar 8;108(5):649-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11893336 11893336] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| Line 23: | Line 32: | ||
[[Category: calcium-dependent cysteine protease]] | [[Category: calcium-dependent cysteine protease]] | ||
[[Category: papain-related]] | [[Category: papain-related]] | ||
| - | [[Category: two novel cooperative calcium | + | [[Category: two novel cooperative calcium site]] |
| - | ''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 12:23:36 2008'' |
Revision as of 10:23, 20 March 2008
| |||||||
| , resolution 2.07Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CAPN1 (Rattus norvegicus) | ||||||
| Activity: | Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Calcium-Bound Protease Core of Calpain I
Overview
Ca(2+) signaling by calpains leads to controlled proteolysis during processes ranging from cytoskeleton remodeling in mammals to sex determination in nematodes. Deregulated Ca(2+) levels result in aberrant proteolysis by calpains, which contributes to tissue damage in heart and brain ischemias as well as neurodegeneration in Alzheimer's disease. Here we show that activation of the protease core of mu calpain requires cooperative binding of two Ca(2+) atoms at two non-EF-hand sites revealed in the 2.1 A crystal structure. Conservation of the Ca(2+) binding residues defines an ancestral general mechanism of activation for most calpain isoforms, including some that lack EF-hand domains. The protease region is not affected by the endogenous inhibitor, calpastatin, and may contribute to calpain-mediated pathologies when the core is released by autoproteolysis.
About this Structure
1KXR is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
A Ca(2+) switch aligns the active site of calpain., Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL, Cell. 2002 Mar 8;108(5):649-60. PMID:11893336
Page seeded by OCA on Thu Mar 20 12:23:36 2008
