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{{Theoretical_model}} | |||
==HOMOLOGY-BASED MODEL OF A HOMO-DIMER OF HUMAN CALPAIN 3 (P94) PENTA-EF HAND DOMAIN (DOMAIN IV)== | |||
<StructureSection load='1y9v' size='340' side='right'caption='[[1y9v]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9V FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y9v FirstGlance], [https://www.ebi.ac.uk/pdbsum/1y9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9v ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Calpains 1 and 2 are heterodimeric proteases in which large (relative molecular mass M(r) 80000) and small (M(r) 28000) subunits are linked through their respective PEF (penta-EF-hand) domains. The skeletal muscle-specific calpain 3 is believed not to form a heterodimer with the small subunit but might homodimerize through its PEF domain. Size-exclusion chromatography and analytical ultracentrifugation of the recombinant PEF domain of calpain 3 show that it forms a stable homodimer that does not dissociate on dilution. Molecular modelling suggests that there would be no barriers to the dimerization of the whole enzyme through the PEF domains. This orientation would place the catalytic centres at opposite ends of the dimer. | |||
Homodimerization of calpain 3 penta-EF-hand domain.,Ravulapalli R, Diaz BG, Campbell RL, Davies PL Biochem J. 2005 Jun 1;388(Pt 2):585-91. PMID:15660530<ref>PMID:15660530</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1y9v" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Campbell, R L]] | |||
[[Category: Davies, P L]] | |||
[[Category: Garcia Diaz, B]] | |||
[[Category: Ravulapalli, R]] | |||
Latest revision as of 19:25, 3 November 2021
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HOMOLOGY-BASED MODEL OF A HOMO-DIMER OF HUMAN CALPAIN 3 (P94) PENTA-EF HAND DOMAIN (DOMAIN IV)HOMOLOGY-BASED MODEL OF A HOMO-DIMER OF HUMAN CALPAIN 3 (P94) PENTA-EF HAND DOMAIN (DOMAIN IV)
Structural highlights
Publication Abstract from PubMedCalpains 1 and 2 are heterodimeric proteases in which large (relative molecular mass M(r) 80000) and small (M(r) 28000) subunits are linked through their respective PEF (penta-EF-hand) domains. The skeletal muscle-specific calpain 3 is believed not to form a heterodimer with the small subunit but might homodimerize through its PEF domain. Size-exclusion chromatography and analytical ultracentrifugation of the recombinant PEF domain of calpain 3 show that it forms a stable homodimer that does not dissociate on dilution. Molecular modelling suggests that there would be no barriers to the dimerization of the whole enzyme through the PEF domains. This orientation would place the catalytic centres at opposite ends of the dimer. Homodimerization of calpain 3 penta-EF-hand domain.,Ravulapalli R, Diaz BG, Campbell RL, Davies PL Biochem J. 2005 Jun 1;388(Pt 2):585-91. PMID:15660530[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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