9I63

Synthetic Human Saposin D glycoprotein

Summary for 9I63

• Entry DOI: 10.2210/pdb9i63/pdb
• Related: 2r0r 2r1q 2rb3 3bqp 3bqq 5u85
• Descriptor: Prosaposin, SULFATE ION (3 entities in total)
• Functional Keywords: glycoprotein, ligation, lipid metabolism, n-glycan, lipid binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 18331.10

Authors

Weyand, M.,Unverzagt, C. (deposition date: 2025-01-29, release date: 2025-04-09)

Primary citation

Graf, C.G.F.,Schulz, C.,Schmalzlein, M.,Heinlein, C.,Monnich, M.,Perkams, L.,Puttner, M.,Boos, I.,Hessefort, M.,Lombana Sanchez, J.N.,Weyand, M.,Steegborn, C.,Breiden, B.,Ross, K.,Schwarzmann, G.,Sandhoff, K.,Unverzagt, C.
Synthetic Glycoforms Reveal Carbohydrate-Dependent Bioactivity of Human Saposin D.
Angew.Chem.Int.Ed.Engl., 56:5252-5257, 2017

PubMed Abstract: The main glycoforms of the hydrophobic lysosomal glycoprotein saposin D (SapD) were synthesized by native chemical ligation. An approach for the challenging solid-phase synthesis of the fragments was developed. Three SapD glycoforms were obtained following a general and robust refolding and purification protocol. A crystal structure of one glycoform confirmed its native structure and disulfide pattern. Functional assays revealed that the lipid-binding properties of three SapD glycoforms are highly affected by the single sugar moiety of SapD showing a dependency of the size and the type of N-glycan.

PubMed: 28378443
DOI: 10.1002/anie.201701362

Experimental method

X-RAY DIFFRACTION (1.65 Å)