scholarly journals A non-canonical binding interface in the crystal structure of HIV-1 gp120 core in complex with CD4

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Liang-Wei Duan ◽  
Hui Zhang ◽  
Meng-Ting Zhao ◽  
Ji-Xue Sun ◽  
Wen-Li Chen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Interface ◽  
Gp120 Core ◽  
Hiv 1

Crystal structure of the Vif-interaction domain of the anti-viral APOBE3F

2014 ◽  
Vol 70 (a1) ◽  
pp. C123-C123
Author(s):  
Masaaki Nakashima ◽  
Shingo Kitamura ◽  
Teppei Kurosawa ◽  
Hirotaka Ode ◽  
Takashi Kawamura ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mutational Analysis ◽  
Structural Features ◽  
Interaction Domain ◽  
Structure Information ◽  
Binding Interface ◽  
Interaction Interface ◽  
Extended Area ◽  
Anti Hiv ◽  
Hiv 1

Human cells express a family of cytidine deaminases, called APOBEC3 (A3) (A3A, B, C, D, F, G, and H). The family enzymes, especially A3G and A3F potentially inhibit replication of retroviruses including HIV-1. However, HIV-1 overcomes the A3-mediated antiviral system by expressing a virus-encoded antagonist, viral infectivity factor (Vif) protein. In HIV-1-infected cells, Vif specifically binds with A3 followed by proteasomal degradation of A3. Hence, inhibition of the interaction between A3 and Vif is an attractive strategy for developing novel anti-HIV-1 drugs. To date, we have determined the first crystal structure of A3 with Vif-binding interface, A3C (PDB ID: 3VOW). In addition, our extensive mutational analysis, based on the A3C structure, revealed that structural features of the Vif-binding interface are highly conserved among A3C, DE, and F [1]. However, more recently, Bohn et al. and Karen et al. have shown the crystal structures of mutant A3F C-terminal domain (CTD) which is responsible for the Vif interaction, and have predicted more extended area, including our identified residues, for the interface on the A3F CTD [2][3]. To clarify the Vif-binding interface of A3F, we sought to determine the crystal structure of the wild-type A3F CTD and evaluated contributions of the additional residues for the Vif-interaction interface by virological method. First, we have successfully determined the crystal structure of A3F CTD at 2.75 Å resolution. Furthermore, we have identified four additional residues unique on the A3F CTD but not A3C for Vif interaction, which are located in the vicinity of our previously reported interface. These results demonstrated that the structural features of Vif-binding interface are indeed conserved between A3C and A3F. Taken together, these results will provide the fine-tuned structure information to understand the binding between A3 and Vif and to facilitate a development of novel anti-HIV-1 compounds targeting A3 proteins.

scholarly journals Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450

1996 ◽  
Vol 3 (4) ◽  
pp. 301-314 ◽  
Author(s):  
C. Nicholas Hodge ◽  
Paul E. Aldrich ◽  
Lee T. Bacheler ◽  
Chong-Hwan Chang ◽  
Charles J. Eyermann ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Human Pharmacokinetics ◽  
Resistance Profile ◽  
X Ray ◽  
Hiv 1

Crystal Structure of HIV-1 Reverse Transcriptase Bound to a Non-Nucleoside Inhibitor with a Novel Mechanism of Action

2010 ◽  
Vol 122 (10) ◽  
pp. 1849-1852 ◽  
Author(s):  
Séverine Freisz ◽  
Guillaume Bec ◽  
Marco Radi ◽  
Philippe Wolff ◽  
Emmanuele Crespan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Reverse Transcriptase ◽  
Mechanism Of Action ◽  
Hiv 1

scholarly journals Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation

2018 ◽  
Vol 116 (2) ◽  
pp. 528-533 ◽  
Author(s):  
Ivan B. Lomakin ◽  
Sergey E. Dmitriev ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Translation Initiation ◽  
Zinc Ion ◽  
Zinc Binding ◽  
Ion Binding ◽  
Binding Interface ◽  
Zinc Binding Site ◽  
Reading Frames ◽  
Zinc Ion Binding

The density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein support noncanonical translation initiation, promote translation reinitiation on a specific set of mRNAs with short upstream reading frames, and regulate ribosome recycling. DENR and MCT-1 form a heterodimer, which binds to the ribosome. We determined the crystal structure of the heterodimer formed by human MCT-1 and the N-terminal domain of DENR at 2.0-Å resolution. The structure of the heterodimer reveals atomic details of the mechanism of DENR and MCT-1 interaction. Four conserved cysteine residues of DENR (C34, C37, C44, C53) form a classical tetrahedral zinc ion-binding site, which preserves the structure of the DENR’s MCT-1–binding interface that is essential for the dimerization. Substitution of all four cysteines by alanine abolished a heterodimer formation. Our findings elucidate further the mechanism of regulation of DENR-MCT-1 activities in unconventional translation initiation, reinitiation, and recycling.

Crystal Structure of the Broadly Cross-Reactive HIV-1-Neutralizing Fab X5 and Fine Mapping of Its Epitope†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (6) ◽  
pp. 1410-1417 ◽  
Author(s):  
Ramalakshmi Darbha ◽  
Sanjay Phogat ◽  
Aran F. Labrijn ◽  
Yuuei Shu ◽  
Yijun Gu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Fine Mapping ◽  
Hiv 1
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