1u5i: Difference between revisions

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[[Image:1u5i.gif|left|200px]]
{{Seed}}
[[Image:1u5i.png|left|200px]]


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{{STRUCTURE_1u5i|  PDB=1u5i  |  SCENE=  }}  
{{STRUCTURE_1u5i|  PDB=1u5i  |  SCENE=  }}  


'''Crystal Structure analysis of rat m-calpain mutant Lys10 Thr'''
===Crystal Structure analysis of rat m-calpain mutant Lys10 Thr===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15476820}}


==About this Structure==
==About this Structure==
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[[Category: Crystal structure]]
[[Category: Crystal structure]]
[[Category: Sulfhydryl protease]]
[[Category: Sulfhydryl protease]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:46:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:22:23 2008''

Revision as of 10:22, 29 July 2008

File:1u5i.png

Template:STRUCTURE 1u5i

Crystal Structure analysis of rat m-calpain mutant Lys10 Thr

Template:ABSTRACT PUBMED 15476820

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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