1JSN

STRUCTURE OF AVIAN H5 HAEMAGGLUTININ COMPLEXED WITH LSTA RECEPTRO ANALOG

1JSN の概要

• エントリーDOI: 10.2210/pdb1jsn/pdb
• 関連するPDBエントリー: 1JSD 1JSH 1JSI 1JSM 1JSO
• 分子名称: HAEMAGGLUTININ (HA1 CHAIN), HAEMAGGLUTININ (HA2 CHAIN), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: influenza, receptor complex, fusion protein, viral protein
• 由来する生物種: Influenza A virus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58960.47

構造登録者

Ha, Y.,Stevens, D.J.,Skehel, J.J.,Wiley, D.C. (登録日: 2001-08-17, 公開日: 2001-09-26, 最終更新日: 2024-10-16)

主引用文献

Ha, Y.,Stevens, D.J.,Skehel, J.J.,Wiley, D.C.
X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs.
Proc.Natl.Acad.Sci.USA, 98:11181-11186, 2001

PubMed Abstract: The three-dimensional structures of avian H5 and swine H9 influenza hemagglutinins (HAs) from viruses closely related to those that caused outbreaks of human disease in Hong Kong in 1997 and 1999 were determined bound to avian and human cell receptor analogs. Emerging influenza pandemics have been accompanied by the evolution of receptor-binding specificity from the preference of avian viruses for sialic acid receptors in alpha2,3 linkage to the preference of human viruses for alpha2,6 linkages. The four new structures show that HA binding sites specific for human receptors appear to be wider than those preferring avian receptors and how avian and human receptors are distinguished by atomic contacts at the glycosidic linkage. alpha2,3-Linked sialosides bind the avian HA in a trans conformation to form an alpha2,3 linkage-specific motif, made by the glycosidic oxygen and 4-OH of the penultimate galactose, that is complementary to the hydrogen-bonding capacity of Gln-226, an avian-specific residue. alpha2,6-Linked sialosides bind in a cis conformation, exposing the glycosidic oxygen to solution and nonpolar atoms of the receptor to Leu-226, a human-specific residue. The new structures are compared with previously reported crystal structures of HA/sialoside complexes of the H3 subtype that caused the 1968 Hong Kong Influenza virus pandemic and analyzed in relation to HA sequences of all 15 subtypes and to receptor affinity data to make clearer how receptor-binding sites of HAs from avian viruses evolve as the virus adapts to humans.

PubMed: 11562490
DOI: 10.1073/pnas.201401198

実験手法

X-RAY DIFFRACTION (2.4 Å)