6L1Y

structure of gp120/CD4 with a non-canonical surface

Summary for 6L1Y

• Entry DOI: 10.2210/pdb6l1y/pdb
• Descriptor: gp120, T-cell surface glycoprotein CD4, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: hiv, gp120, cd4 receptor, protein binding
• Biological source: Human immunodeficiency virus 1; More
• Total number of polymer chains: 2
• Total formula weight: 65002.76

Authors

Liu, X.,Ning, W. (deposition date: 2019-10-01, release date: 2020-05-20, Last modification date: 2024-11-13)

Primary citation

Duan, L.W.,Zhang, H.,Zhao, M.T.,Sun, J.X.,Chen, W.L.,Lin, J.P.,Liu, X.Q.
A non-canonical binding interface in the crystal structure of HIV-1 gp120 core in complex with CD4.
Sci Rep, 7:46733-46733, 2017

PubMed Abstract: Numerous crystal structures of HIV gp120 have been reported, alone or with receptor CD4 and cognate antibodies; however, no sole gp120/CD4 complex without stabilization by an antibody is available. Here, we report a crystal structure of the gp120/CD4 complex without the aid of an antibody from HIV-1 CRF07_BC, a strain circulating in China. Interestingly, in addition to the canonical binding surface, a second interacting interface was identified. A mutagenesis study on critical residues revealed that the stability of this interface is important for the efficiency of Env-mediated membrane fusion. Furthermore, we found that a broad neutralizing antibody, ibalizumab, which targets CD4 in the absence of gp120, occupies the same binding surface as the second interface identified here on gp120. Therefore, we identified the possibility of the involvement of a second gp120-CD4 interaction interface during viral entry, and also provided a reasonable explanation for the broad activity of neutralizing antibody ibalizumab.

PubMed: 28429756
DOI: 10.1038/srep46733

Experimental method

X-RAY DIFFRACTION (2.469 Å)