2EVD

Crystal structure of human Glycolipid Transfer Protein complexed with 12:0 Lactosylceramide

2EVD の概要

• エントリーDOI: 10.2210/pdb2evd/pdb
• 関連するPDBエントリー: 2EUM
• 関連するBIRD辞書のPRD_ID: PRD_900004
• 分子名称: Glycolipid transfer protein, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, SPHINGOSINE, ... (7 entities in total)
• 機能のキーワード: protein-glycolipid complex, lipid transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24976.39

構造登録者

Malinina, L.,Malakhova, M.L.,Kanack, A.T.,Abagyan, R.,Brown, R.E.,Patel, D.J. (登録日: 2005-10-31, 公開日: 2006-11-14, 最終更新日: 2023-08-23)

主引用文献

Malinina, L.,Malakhova, M.L.,Kanack, A.T.,Lu, M.,Abagyan, R.,Brown, R.E.,Patel, D.J.
The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.
Plos Biol., 4:e362-e362, 2006

PubMed Abstract: Glycosphingolipids (GSLs) play major roles in cellular growth and development. Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell processes mediated by GSLs and display a unique architecture among lipid binding/transfer proteins. The GLTP fold represents a novel membrane targeting/interaction domain among peripheral proteins. Here we report crystal structures of human GLTP bound to GSLs of diverse acyl chain length, unsaturation, and sugar composition. Structural comparisons show a highly conserved anchoring of galactosyl- and lactosyl-amide headgroups by the GLTP recognition center. By contrast, acyl chain chemical structure and occupancy of the hydrophobic tunnel dictate partitioning between sphingosine-in and newly-observed sphingosine-out ligand-binding modes. The structural insights, combined with computed interaction propensity distributions, suggest a concerted sequence of events mediated by GLTP conformational changes during GSL transfer to and/or from membranes, as well as during GSL presentation and/or transfer to other proteins.

PubMed: 17105344
DOI: 10.1371/journal.pbio.0040362

実験手法

X-RAY DIFFRACTION (2 Å)