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2BF1

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

Summary for 2BF1
Entry DOI10.2210/pdb2bf1/pdb
DescriptorEXTERIOR 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)
Functional Keywordsvirus protein, siv, gp120, envelope glycoprotein, aids, coat protein
Biological sourceSIMIAN IMMUNODEFICIENCY VIRUS (SIV)
Total number of polymer chains1
Total formula weight46048.21
Authors
Chen, B.,Vogan, E.M.,Gong, H.,Skehel, J.J.,Wiley, D.C.,Harrison, S.C. (deposition date: 2004-12-02, release date: 2005-02-17, Last modification date: 2024-10-16)
Primary citationChen, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4 Å)
Structure validation

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数据于2025-06-18公开中

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