The Potent Anti-HIV Protein Cyanovirin-N Contains Two Novel Carbohydrate Binding Sites That Selectively Bind to Man8 D1D3 and Man9 with Nanomolar Affinity: Implications for Binding to the HIV Envelope Protein gp120-Reference-Cited by-同舟云学术

The Potent Anti-HIV Protein Cyanovirin-N Contains Two Novel Carbohydrate Binding Sites That Selectively Bind to Man8 D1D3 and Man9 with Nanomolar Affinity: Implications for Binding to the HIV Envelope Protein gp120

Published:2001-04-04 Issue:17 Volume:123 Page:3892-3902
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Bewley Carole A.¹,Otero-Quintero Sarah¹

Affiliation:

1. Contribution from the Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0820

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja004040e

Reference42 articles.

1. Cyanovirin-N Binds to gp120 To Interfere with CD4-Dependent Human Immunodeficiency Virus Type 1 Virion Binding, Fusion, and Infectivity but Does Not Affect the CD4 Binding Site on gp120 or Soluble CD4-Induced Conformational Changes in gp120

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