Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies-Reference-Cited by-同舟云学术

Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies

Published:2013-11-13 Issue:47 Volume:135 Page:17793-17803
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Han Yun¹,Hou Guangjin¹,Suiter Christopher L.¹,Ahn Jinwoo,Byeon In-Ja L.,Lipton Andrew S.²,Burton Sarah²,Hung Ivan³,Gor′kov Peter L.³,Gan Zhehong³,Brey William³,Rice David⁴,Gronenborn Angela M.,Polenova Tatyana¹

Affiliation:

1. Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States

2. Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington, 99352, United States

3. National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida, 32310, United States

4. Agilent Technologies, Inc., Santa Clara, California 95051, United States

Funder

National Science Foundation

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja406907h

Reference44 articles.

1. The HIV-1 assembly machine

2. The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions

3. HIV-1 Assembly, Budding, and Maturation

4. Structural organization of authentic, mature HIV-1 virions and cores

5. Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice

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