1mdw
From Proteopedia
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| - | [[Image:1mdw.gif|left|200px]] | + | [[Image:1mdw.gif|left|200px]] |
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| - | '''Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation''' | + | {{Structure |
| + | |PDB= 1mdw |SIZE=350|CAPTION= <scene name='initialview01'>1mdw</scene>, resolution 1.95Å | ||
| + | |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= CALPAIN II ([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 II Reveals the Basis for Intrinsic Inactivation''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MDW is a [ | + | 1MDW 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=1MDW OCA]. |
==Reference== | ==Reference== | ||
| - | Calpain silencing by a reversible intrinsic mechanism., Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL, Nat Struct Biol. 2003 May;10(5):371-8. PMID:[http:// | + | Calpain silencing by a reversible intrinsic mechanism., Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL, Nat Struct Biol. 2003 May;10(5):371-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12665854 12665854] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: helix instability]] | [[Category: helix instability]] | ||
[[Category: tryptophan-based active site blockage]] | [[Category: tryptophan-based active site blockage]] | ||
| - | [[Category: two cooperative calcium | + | [[Category: two 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 12:42:19 2008'' |
Revision as of 10:42, 20 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CALPAIN II (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 II Reveals the Basis for Intrinsic Inactivation
Overview
Uncontrolled activation of calpain can lead to necrotic cell death and irreversible tissue damage. We have discovered an intrinsic mechanism whereby the autolysis-generated protease core fragment of calpain is inactivated through the inherent instability of a key alpha-helix. This auto-inactivation state was captured by the 1.9 A Ca(2+)-bound structure of the protease core from m-calpain, and sequence alignments suggest that it applies to about half of the calpain isoforms. Intact calpain large subunits are also subject to this inhibition, which can be prevented through assembly of the heterodimers. Other isoforms or their released cores are not silenced by this mechanism and might contribute to calpain patho-physiologies.
About this Structure
1MDW is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Calpain silencing by a reversible intrinsic mechanism., Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL, Nat Struct Biol. 2003 May;10(5):371-8. PMID:12665854
Page seeded by OCA on Thu Mar 20 12:42:19 2008
