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| [[Image:1qxp.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1qxp| PDB=1qxp | SCENE= }} | | {{STRUCTURE_1qxp| PDB=1qxp | SCENE= }} |
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| '''Crystal Structure of a mu-like calpain'''
| | ===Crystal Structure of a mu-like calpain=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_14656436}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14656436 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14656436}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: M-calpain]] | | [[Category: M-calpain]] |
| [[Category: Mu-calpain]] | | [[Category: Mu-calpain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:49:46 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:07:34 2008'' |