4YWT

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

4YWT の概要

• エントリーDOI: 10.2210/pdb4ywt/pdb
• 関連するPDBエントリー: 4ad7
• 分子名称: Glypican-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: glypican-1, diffraction quality, controlled dehydration, hc1b, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 235273.43

構造登録者

Awad, W.,Mani, K.,Logan, D.T. (登録日: 2015-03-21, 公開日: 2015-07-29, 最終更新日: 2024-11-13)

主引用文献

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

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: 26203194
DOI: 10.1074/jbc.M115.660878

実験手法

X-RAY DIFFRACTION (2.38 Å)