1sn6
From Proteopedia
NMR solution structure of human Saposin C in SDS micelles
Contents |
Overview
Saposin C is a lysosomal, membrane-binding protein that acts as an activator for the hydrolysis of glucosylceramide by the enzyme glucocerebrosidase. We used high-resolution NMR to determine the three-dimensional solution structure of saposin C in the presence of the detergent sodium dodecyl sulfate (SDS). This structure provides the first representation of membrane bound saposin C at the atomic level. In the presence of SDS, the protein adopts an open conformation with an exposed hydrophobic pocket. In contrast, the previously reported NMR structure of saposin C in the absence of SDS is compact and contains a hydrophobic core that is not exposed to the solvent. NMR data indicate that the SDS molecules interact with the hydrophobic pocket. The structure of saposin C in the presence of SDS is very similar to a monomer in the saposin B homodimer structure. Their comparison reveals possible similarity in the type of protein/lipid interaction as well as structural components differentiating their quaternary structures and functional specificity.
Disease
Known disease associated with this structure: Combined SAP deficiency OMIM:[176801], Gaucher disease, atypical OMIM:[176801], Krabbe disease, atypical OMIM:[176801], Metachromatic leukodystrophy due to SAP-b deficiency OMIM:[176801]
About this Structure
1SN6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human saposin C in a detergent environment., Hawkins CA, de Alba E, Tjandra N, J Mol Biol. 2005 Mar 11;346(5):1381-92. Epub 2005 Jan 20. PMID:15713488 Page seeded by OCA on Sat May 3 08:54:45 2008
