Saposin
From Proteopedia
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| - | {{STRUCTURE_2dob| PDB=2dob | SIZE=400| SCENE= |right|CAPTION=Human saposin | + | {{STRUCTURE_2dob| PDB=2dob | SIZE=400| SCENE= |right|CAPTION=Human saposin A complex with Ca+2 ion, [[2dob]] }} |
'''Saposin''' (Sap) is a small protein which functions as activator of lipid-degrading enzymes. They act by isolating the lipid substrate from the membrane. Sap is synthesized as a precursor – prosaposin – which contain 4 SapB active domains and 2 SapA domains which are cleaved off. For more details see [[Molecular Playground/Saposin C]]. | '''Saposin''' (Sap) is a small protein which functions as activator of lipid-degrading enzymes. They act by isolating the lipid substrate from the membrane. Sap is synthesized as a precursor – prosaposin – which contain 4 SapB active domains and 2 SapA domains which are cleaved off. For more details see [[Molecular Playground/Saposin C]]. | ||
Revision as of 12:21, 14 November 2012
Saposin (Sap) is a small protein which functions as activator of lipid-degrading enzymes. They act by isolating the lipid substrate from the membrane. Sap is synthesized as a precursor – prosaposin – which contain 4 SapB active domains and 2 SapA domains which are cleaved off. For more details see Molecular Playground/Saposin C.
3D Structures of Saposin
Saposin A
2dob – hSapA residues 60-140 – human
Saposin B
1n69 – hSapB + lipid
Saposin C
1m12, 1sn6 – hSapC – NMR
2gtg, 2qyp, 2z9a – hSapC residues 311-391
Saposin D
3bqp, 3bqq, 2r1q, 2rb3 - hSapD residues 405-484
2r0r - hSapD residues 407-484 (mutant)
