1u5i
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Calpain-2 Calpain-2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.53 3.4.22.53] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Calpain-2 Calpain-2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.53 3.4.22.53] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1df0|1DF0]], [[1qxp|1QXP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u5i OCA], [http://www.ebi.ac.uk/pdbsum/1u5i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u5i RCSB]</span> | ||
}} | }} | ||
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[[Category: sulfhydryl protease]] | [[Category: sulfhydryl protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:05:36 2008'' |
Revision as of 21:05, 30 March 2008
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| , resolution 2.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Calpain-2, with EC number 3.4.22.53 | ||||||
| Related: | 1DF0, 1QXP
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure analysis of rat m-calpain mutant Lys10 Thr
Overview
The calpains are a family of cysteine proteases with closely related amino acid sequences, but a wide range of Ca(2+) requirements (K(d)). For m-calpain, K(d) is approximately 325microM, for mu-calpain it is approximately 50microM, and for calpain 3 it is not strictly known but may be approximately 0.1microM. On the basis of previous structure determination of m-calpain we postulated that two regions of the calpain large subunits, the N-terminal peptide (residues 1-20) and a domain III-IV linker peptide (residues 514-530 in m-calpain) were important in defining K(d). The mutations Lys10Thr in the N-terminal peptide, and Glu517Pro in the domain linker peptide, reduced K(d) of m-calpain by 30% and 42%, respectively, revealing that these two regions are functionally important. The increased Ca(2+)-sensitivity of these mutants demonstrate that the Lys10-Asp148 salt link and the short beta-sheet interaction involving Glu517 are factors contributing to the high K(d) of m-calpain. Though these two regions are physically remote from the active site and Ca(2+)-binding site, they play significant roles in regulating the response of calpain to Ca(2+). Differences in these interactions in mu-calpain and in calpain 3 are also consistent with their progressively lower K(d) values.
About this Structure
1U5I is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Activation of calpain by Ca2+: roles of the large subunit N-terminal and domain III-IV linker peptides., Hosfield CM, Elce JS, Jia Z, J Mol Biol. 2004 Oct 29;343(4):1049-53. PMID:15476820
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