1qxp
From Proteopedia
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| - | [[Image:1qxp.jpg|left|200px]] | + | [[Image:1qxp.jpg|left|200px]] |
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| - | '''Crystal Structure of a mu-like calpain''' | + | {{Structure |
| + | |PDB= 1qxp |SIZE=350|CAPTION= <scene name='initialview01'>1qxp</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Calpain-1 Calpain-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 3.4.22.52] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of a mu-like calpain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QXP is a [ | + | 1QXP 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=1QXP OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement., Pal GP, De Veyra T, Elce JS, Jia Z, Structure. 2003 Dec;11(12):1521-6. PMID:[http:// | + | Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement., Pal GP, De Veyra T, Elce JS, Jia Z, Structure. 2003 Dec;11(12):1521-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14656436 14656436] |
[[Category: Calpain-1]] | [[Category: Calpain-1]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: mu-calpain]] | [[Category: mu-calpain]] | ||
| - | ''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 13:44:07 2008'' |
Revision as of 11:44, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Activity: | Calpain-1, with EC number 3.4.22.52 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a mu-like calpain
Overview
The two Ca2+-dependent cysteine proteases, micro- and m-calpain, are involved in various Ca2+-linked signal pathways but differ markedly in their Ca2+ requirements for activation. We have determined the structure of a micro-like calpain, which has 85% micro-calpain sequence (the first 48 and the last 62 residues of the large subunit are those from m-calpain) and a low Ca2+ requirement. This construct was used because micro-calpain itself is too poorly expressed. The structure of micro-like calpain is very similar in overall fold to that of m-calpain as expected, but differs significantly in two aspects. In comparison with m-calpain, the catalytic triad residues in micro-like calpain, His and Cys, are much closer together in the absence of Ca2+, and significant portions of the Ca2+ binding EF-hand motifs are disordered and more flexible. These structural differences imply that Ca2+-free micro-calpain may represent a partially activated structure, requiring lower Ca2+ concentration to trigger its activation.
About this Structure
1QXP is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement., Pal GP, De Veyra T, Elce JS, Jia Z, Structure. 2003 Dec;11(12):1521-6. PMID:14656436
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