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1u5i

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[[Image:1u5i.gif|left|200px]]
[[Image:1u5i.gif|left|200px]]
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{{Structure
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|PDB= 1u5i |SIZE=350|CAPTION= <scene name='initialview01'>1u5i</scene>, resolution 2.86&Aring;
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The line below this paragraph, containing "STRUCTURE_1u5i", creates the "Structure Box" on the page.
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|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>
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{{STRUCTURE_1u5i| PDB=1u5i | SCENE= }}
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|RELATEDENTRY=[[1df0|1DF0]], [[1qxp|1QXP]]
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|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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'''Crystal Structure analysis of rat m-calpain mutant Lys10 Thr'''
'''Crystal Structure analysis of rat m-calpain mutant Lys10 Thr'''
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[[Category: Jia, Z.]]
[[Category: Jia, Z.]]
[[Category: Pal, G P.]]
[[Category: Pal, G P.]]
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[[Category: calpain]]
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[[Category: Calpain]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: sulfhydryl protease]]
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[[Category: Sulfhydryl protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:46:51 2008''
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Revision as of 07:46, 3 May 2008

Template:STRUCTURE 1u5i

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 Page seeded by OCA on Sat May 3 10:46:51 2008

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