Crystal structures of saposins A and C. [Protein Sci. 2006]

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1: Protein Sci. 2006 Aug;15(8):1849-57. Epub 2006 Jul 5. Links

Crystal structures of saposins A and C.

Ahn VE, Leyko P, Alattia JR, Chen L, Privé GG.

Department of Medical Biophysics, University of Toronto, Canada.

Saposins A and C are sphingolipid activator proteins required for the lysosomal breakdown of galactosylceramide and glucosylceramide, respectively. The saposins interact with lipids, leading to an enhanced accessibility of the lipid headgroups to their cognate hydrolases. We have determined the crystal structures of human saposins A and C to 2.0 Angstroms and 2.4 Angstroms, respectively, and both reveal the compact, monomeric saposin fold. We confirmed that these two proteins were monomeric in solution at pH 7.0 by analytical centrifugation. However, at pH 4.8, in the presence of the detergent C(8)E(5), saposin A assembled into dimers, while saposin C formed trimers. Saposin B was dimeric under all conditions tested. The self-association of the saposins is likely to be relevant to how these small proteins interact with lipids, membranes, and hydrolase enzymes.

PMID: 16823039 [PubMed - indexed for MEDLINE]

PMCID: PMC2242594

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Acta Crystallogr D Biol Crystallogr. 2008 May; 64(Pt 5):589-94. Epub 2008 Apr 19.

[Acta Crystallogr D Biol Crystallogr. 2008]
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[Proc Natl Acad Sci U S A. 2003]
ReviewSaposins and their interaction with lipids.
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[Neurochem Res. 1999]
ReviewSaposin proteins: structure, function, and role in human lysosomal storage disorders.
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[FASEB J. 1991]
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Cited by 3 PubMed Central articles

Molecular imaging of membrane interfaces reveals mode of beta-glucosidase activation by saposin C.
Alattia JR, Shaw JE, Yip CM, Privé GG. Proc Natl Acad Sci U S A. 2007 Oct 30; 104(44):17394-9. Epub 2007 Oct 22.

[Proc Natl Acad Sci U S A. 2007]
Investigating the interaction of saposin C with POPS and POPC phospholipids: a solid-state NMR spectroscopic study.
Abu-Baker S, Qi X, Lorigan GA. Biophys J. 2007 Nov 15; 93(10):3480-90. Epub 2007 Aug 17.

[Biophys J. 2007]
Saposin B is the dominant saposin that facilitates lipid binding to human CD1d molecules.
Yuan W, Qi X, Tsang P, Kang SJ, Illarionov PA, Besra GS, Gumperz J, Cresswell P. Proc Natl Acad Sci U S A. 2007 Mar 27; 104(13):5551-6. Epub 2007 Mar 19.

[Proc Natl Acad Sci U S A. 2007]

Structures reported by this article

Crystal Structure Of Human Saposin C

PDB: 2GTG

Source: Homo sapiens

Method: X-Ray Diffraction | Resolution: 2.4 Å
» See all 2 structures...

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