2BF1

Structure of an unliganded and fully-glycosylated SIV gp120 envelope glycoprotein

2BF1 の概要

• エントリーDOI: 10.2210/pdb2bf1/pdb
• 分子名称: EXTERIOR MEMBRANE GLYCOPROTEIN GP120, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: virus protein, siv, gp120, envelope glycoprotein, aids, coat protein
• 由来する生物種: SIMIAN IMMUNODEFICIENCY VIRUS (SIV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46048.21

構造登録者

Chen, B.,Vogan, E.M.,Gong, H.,Skehel, J.J.,Wiley, D.C.,Harrison, S.C. (登録日: 2004-12-02, 公開日: 2005-02-17, 最終更新日: 2024-10-16)

主引用文献

Chen, B.,Vogan, E.M.,Gong, H.,Skehel, J.J.,Wiley, D.C.,Harrison, S.C.
Structure of an Unliganded Simian Immunodeficiency Virus Gp120 Core
Nature, 433:834-, 2005

PubMed Abstract: Envelope glycoproteins of human and simian immunodeficiency virus (HIV and SIV) undergo a series of conformational changes when they interact with receptor (CD4) and co-receptor on the surface of a potential host cell, leading ultimately to fusion of viral and cellular membranes. Structures of fragments of gp120 and gp41 from the envelope protein are known, in conformations corresponding to their post-attachment and postfusion states, respectively. We report the crystal structure, at 4 A resolution, of a fully glycosylated SIV gp120 core, in a conformation representing its prefusion state, before interaction with CD4. Parts of the protein have a markedly different organization than they do in the CD4-bound state. Comparison of the unliganded and CD4-bound structures leads to a model for events that accompany receptor engagement of an envelope glycoprotein trimer. The two conformations of gp120 also present distinct antigenic surfaces. We identify the binding site for a compound that inhibits viral entry.

PubMed: 15729334
DOI: 10.1038/NATURE03327

実験手法

X-RAY DIFFRACTION (4 Å)