3A5P

Crystal structure of hemagglutinin

3A5P の概要

• エントリーDOI: 10.2210/pdb3a5p/pdb
• 分子名称: Haemagglutinin I (2 entities in total)
• 機能のキーワード: lectin, sugar binding protein
• 由来する生物種: Physarum polycephalum (Slime mold)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 43600.40

構造登録者

Watanabe, N.,Sakai, N.,Nakamura, T.,Nabeshima, Y.,Kouno, T.,Mizuguchi, M.,Kawano, K. (登録日: 2009-08-10, 公開日: 2010-08-11, 最終更新日: 2024-04-03)

主引用文献

Kouno, T.,Watanabe, N.,Sakai, N.,Nakamura, T.,Nabeshima, Y.,Morita, M.,Mizuguchi, M.,Aizawa, T.,Demura, M.,Imanaka, T.,Tanaka, I.,Kawano, K.
The Structure of Physarum polycephalum hemagglutinin I suggests a minimal carbohydrate recognition domain of legume lectin fold
J.Mol.Biol., 405:560-569, 2011

PubMed Abstract: Physarum polycephalum hemagglutinin I (HA1) is a 104-residue protein that is secreted to extracellular space. The crystal structure of HA1 has a β-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the β-sandwich of HA1 lacks a jelly roll motif and is essentially composed of two simple up-and-down β-sheets. This up-and-down β-sheet motif is well conserved in other legume lectin-like proteins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down β-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that HA1 lacking a jelly roll motif also binds to its target glycopeptide. Taken together, these data show that the up-and-down β-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of HA1 suggests a minimal carbohydrate recognition domain.

PubMed: 21094650
DOI: 10.1016/j.jmb.2010.11.024

実験手法

X-RAY DIFFRACTION (1.82 Å)