1u5i
From Proteopedia
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| - | [[Image:1u5i.gif|left|200px]] | + | [[Image:1u5i.gif|left|200px]] |
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| - | '''Crystal Structure analysis of rat m-calpain mutant Lys10 Thr''' | + | {{Structure |
| + | |PDB= 1u5i |SIZE=350|CAPTION= <scene name='initialview01'>1u5i</scene>, resolution 2.86Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure analysis of rat m-calpain mutant Lys10 Thr''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1U5I is a [ | + | 1U5I is a [[Protein complex]] structure of sequences 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=1U5I OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15476820 15476820] |
[[Category: Calpain-2]] | [[Category: Calpain-2]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: sulfhydryl protease]] | [[Category: sulfhydryl protease]] | ||
| - | ''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 14:27:36 2008'' |
Revision as of 12:27, 20 March 2008
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| , resolution 2.86Å | |||||||
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| Activity: | Calpain-2, with EC number 3.4.22.53 | ||||||
| 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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