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1sn6

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1sn6, 20 NMR models ()
Gene: PSAP (Homo sapiens)
Related: 1m12
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR solution structure of human Saposin C in SDS micelles

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1sn6 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • Hawkins CA, de Alba E, Tjandra N. Solution structure of human saposin C in a detergent environment. J Mol Biol. 2005 Mar 11;346(5):1381-92. Epub 2005 Jan 20. PMID:15713488 doi:10.1016/j.jmb.2004.12.045
  • de Alba E, Weiler S, Tjandra N. Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles. Biochemistry. 2003 Dec 23;42(50):14729-40. PMID:14674747 doi:10.1021/bi0301338

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