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Rhomboid protease

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<StructureSection load='2xow' size='450' side='right' caption='Structure of rhomboid protease complex with inhibitor isocoumarin and nonyglucoside detergent molecules (PDB entry [[2xow]])' scene='55/551211/Cv/1'>
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<StructureSection load='' size='450' side='right' caption='Structure of rhomboid protease complex with inhibitor isocoumarin and nonyglucoside detergent molecules (PDB entry [[2xow]])' scene='55/551211/Cv/1'>
== Function ==
== Function ==
'''Rhomboid protease''' (GlpG) is a transmembranal serine protease. The active site is buried in the lipid bilayer of cell membrane. It cleaves proteins within their transmembrane domain<ref>PMID:18605900</ref>. Rhomboids regulate many cellular processes and are involved in many human diseases. The catalytic site of rhomboids contains a hydrophilic pocket protected from the lipid bilayer. Rhomboids are specific for a single transmembranal helix proteins.
'''Rhomboid protease''' (GlpG) is a transmembranal serine protease. The active site is buried in the lipid bilayer of cell membrane. It cleaves proteins within their transmembrane domain<ref>PMID:18605900</ref>. Rhomboids regulate many cellular processes and are involved in many human diseases. The catalytic site of rhomboids contains a hydrophilic pocket protected from the lipid bilayer. Rhomboids are specific for a single transmembranal helix proteins.

Revision as of 05:57, 22 October 2017

Structure of rhomboid protease complex with inhibitor isocoumarin and nonyglucoside detergent molecules (PDB entry 2xow)

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3D Structures of rhomboid protease

Updated on 22-October-2017

References

  1. Freeman M. Rhomboid proteases and their biological functions. Annu Rev Genet. 2008;42:191-210. doi: 10.1146/annurev.genet.42.110807.091628. PMID:18605900 doi:http://dx.doi.org/10.1146/annurev.genet.42.110807.091628
  2. Vinothkumar KR, Strisovsky K, Andreeva A, Christova Y, Verhelst S, Freeman M. The structural basis for catalysis and substrate specificity of a rhomboid protease. EMBO J. 2010 Oct 1. PMID:20890268 doi:10.1038/emboj.2010.243

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