2CE6

Structure of Helix Pomatia agglutinin with no ligands

2CE6 の概要

• エントリーDOI: 10.2210/pdb2ce6/pdb
• 関連するPDBエントリー: 2CCV
• 分子名称: HELIX POMATIA AGGLUTININ (2 entities in total)
• 機能のキーワード: lectin, snail, helix pomatia
• 由来する生物種: HELIX POMATIA (ROMAN SNAIL)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11338.78

構造登録者

Sanchez, J.-F.,Lescar, J.,Chazalet, V.,Audfray, A.,Gautier, C.,Gagnon, J.,Breton, C.,Imberty, A.,Mitchell, E.P. (登録日: 2006-02-03, 公開日: 2006-05-15, 最終更新日: 2024-11-06)

主引用文献

Sanchez, J.-F.,Lescar, J.,Chazalet, V.,Audfray, A.,Gagnon, J.,Alvarez, R.,Breton, C.,Imberty, A.,Mitchell, E.P.
Biochemical and Structural Analysis of Helix Pomatia Agglutinin. A Hexameric Lectin with a Novel Fold.
J.Biol.Chem., 281:20171-, 2006

PubMed Abstract: Helix pomatia agglutinin (HPA) is a N-acetylgalactosamine (GalNAc) binding lectin found in the albumen gland of the roman snail. As a constituent of perivitelline fluid, HPA protects fertilized eggs from bacteria and is part of the innate immunity system of the snail. The peptide sequence deduced from gene cloning demonstrates that HPA belongs to a family of carbohydrate-binding proteins recently identified in several invertebrates. This domain is also present in discoidin from the slime mold Dictyostelium discoideum. Investigation of the lectin specificity was performed with the use of glycan arrays, demonstrating that several GalNAc-containing oligosaccharides are bound and rationalizing the use of this lectin as a cancer marker. Titration microcalorimetry performed on the interaction between HPA and GalNAc indicates an affinity in the 10(-4) M range with an enthalpy-driven binding mechanism. The crystal structure of HPA demonstrates the occurrence of a new beta-sandwich lectin fold. The hexameric quaternary state was never observed previously for a lectin. The high resolution structure complex of HPA with GalNAc characterizes a new carbohydrate binding site and rationalizes the observed preference for alphaGalNAc-containing oligosaccharides.

PubMed: 16704980
DOI: 10.1074/JBC.M603452200

実験手法

X-RAY DIFFRACTION (2.4 Å)