4YWT
Crystal structure of full-length glypican-1 core protein after controlled crystal dehydration to 87% relative humidity
Summary for 4YWT
| Entry DOI | 10.2210/pdb4ywt/pdb |
| Related | 4ad7 |
| Descriptor | Glypican-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | glypican-1, diffraction quality, controlled dehydration, hc1b, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 235273.43 |
| Authors | Awad, W.,Mani, K.,Logan, D.T. (deposition date: 2015-03-21, release date: 2015-07-29, Last modification date: 2024-01-10) |
| Primary citation | Awad, W.,Adamczyk, B.,Ornros, J.,Karlsson, N.G.,Mani, K.,Logan, D.T. Structural Aspects of N-Glycosylations and the C-terminal Region in Human Glypican-1. J.Biol.Chem., 290:22991-23008, 2015 Cited by PubMed 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. PubMed: 26203194DOI: 10.1074/jbc.M115.660878 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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