Reactome | PSAP(195-273) forms a dimer

PSAP(195-273) forms a dimer

Stable Identifier

R-HSA-9840488

Type

Reaction [binding]

Species

Homo sapiens

Compartment

lysosomal lumen

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Saposin B (PSAP(195-273)) is the only PSAP fragment that forms a dimer. The dimer is disulfide-linked and can switch between two conformations, one of which shows an open hydrophobic pocket, supporting a lipid solubilization mechanism for saposin B, consistent with the observation that saposin B can act as a lipid-transport protein (Vaccaro et al., 1995; Ahn et al., 2002; Ahn et al., 2003).

Literature References

PubMed ID	Title	Journal	Year
12510003	Expression, purification, crystallization, and preliminary X-ray analysis of recombinant human saposin B Ahn, VE, Faull, KF, Whitelegge, JP, Higginson, J, Fluharty, AL, Privé, GG	Protein Expr Purif	2003
7730378	Structural analysis of saposin C and B. Complete localization of disulfide bridges Vaccaro, AM, Salvioli, R, Barca, A, Tatti, M, Ciaffoni, F, Maras, B, Siciliano, R, Zappacosta, F, Amoresano, A, Pucci, P	J Biol Chem	1995
12518053	Crystal structure of saposin B reveals a dimeric shell for lipid binding Ahn, VE, Faull, KF, Whitelegge, JP, Fluharty, AL, Privé, GG	Proc Natl Acad Sci U S A	2003