4YWT: Crystal structure of full-length glypican-1 core protein after controlled crystal dehydration to 87% relative humidity

Citation:
Abstract
Glypicans are multifunctional cell surface proteoglycans involved in several important cellular signaling pathways. Glypican-1 (Gpc1) is the predominant heparan sulfate proteoglycan in the developing and adult human brain. The two N-linked glycans and the C-terminal domain that attach the core protein to the cell membrane are not resolved in the Gpc1 crystal structure. Therefore, we have studied Gpc1 using crystallography, small angle x-ray scattering, and chromatographic approaches to elucidate the composition, structure, and function of the N-glycans and the C terminus and also the topology of Gpc1 with respect to the membrane. The C terminus is shown to be highly flexible in solution, but it orients the core protein transverse to the membrane, directing a surface evolutionarily conserved in Gpc1 orthologs toward the membrane, where it may interact with signaling molecules and/or membrane receptors on the cell surface, or even the enzymes involved in heparan sulfate substitution in the Golgi apparatus. Furthermore, the N-glycans are shown to extend the protein stability and lifetime by protection against proteolysis and aggregation.
PDB ID: 4YWTDownload
MMDB ID: 131297
PDB Deposition Date: 2015/3/21
Updated in MMDB: 2015/10
Experimental Method:
x-ray diffraction
Resolution: 2.38  Å
Source Organism:
Similar Structures:
Biological Unit for 4YWT: monomeric; determined by author and by software (PISA)
Molecular Components in 4YWT
Label Count Molecule
Protein (1 molecule)
1
Glypican-1(Gene symbol: GPC1)
Molecule annotation
Chemicals (3 molecules)
1
1
2
2
* Click molecule labels to explore molecular sequence information.

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