1sn6
From Proteopedia
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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 diseases associated with this structure: Combined SAP deficiency OMIM:[176801], Gaucher disease, atypical OMIM:[176801], Metachromatic leukodystrophy due to deficiency of SAP-1 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 Mon Nov 12 19:15:38 2007
