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

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