2PEL

PEANUT LECTIN

「1PEL」から置き換えられました

2PEL の概要

• エントリーDOI: 10.2210/pdb2pel/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900004 PRD_900008
• 分子名称: PEANUT LECTIN, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: legume lectin, open quaternary structure, carbohydrate specificity, protein crystallography, agglutinin, lectin (agglutinin)
• 由来する生物種: Arachis hypogaea (peanut)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102585.07

構造登録者

Banerjee, R.,Das, K.,Ravishankar, R.,Suguna, K.,Surolia, A.,Vijayan, M. (登録日: 1995-08-23, 公開日: 1996-12-07, 最終更新日: 2024-02-21)

主引用文献

Banerjee, R.,Das, K.,Ravishankar, R.,Suguna, K.,Surolia, A.,Vijayan, M.
Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex.
J.Mol.Biol., 259:281-296, 1996

PubMed Abstract: The structure of the complex of the tetrameric peanut lectin with lactose has been refined to an R-value of 16.4% using 2.25 angstroms resolution X-ray diffraction data. The subunit conformation in the structure is similar to that in other legume lectins except in the loops. It has been shown that in the tertiary structure of legume lectins, the short five-stranded sheet plays a major role in connecting the larger flat six-stranded and curved seven-stranded sheets. Furthermore, the loops that connect the strands at the two ends of the seven-stranded sheet curve toward and interact with each other to produce a second hydrophobic core in addition to the one between the two large sheets. The protein-lactose interactions involve the invariant features observed in other legume lectins in addition to those characteristic of peanut lectin. The "open" quaternary association in peanut lectin is stabilised by hydrophobic, hydrogen-bonded and water-mediated interactions. Contrary to the earlier belief, the structure of peanut lectin demonstrates that the variability in quaternary association in legume lectins, despite all of them having nearly the same tertiary structure, is not necessarily caused by covalently bound carbohydrate. An attempt has been made to provide a structural rationale for this variability, on the basis of buried surface areas during dimerisation. A total of 45 water molecules remain invariant when the hydration shells of the four subunits are compared. A majority of them appear to be involved in stabilising loops.

PubMed: 8656429
DOI: 10.1006/jmbi.1996.0319

実験手法

X-RAY DIFFRACTION (2.25 Å)