5GQQ

Structure of ALG-2/HEBP2 Complex

Summary for 5GQQ

• Entry DOI: 10.2210/pdb5gqq/pdb
• Descriptor: Heme-binding protein 2, Programmed cell death protein 6, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: ef hands, complex, calcium ions, apoptosis
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : Q9Y5Z4; Endoplasmic reticulum membrane ; Peripheral membrane protein : O75340
• Total number of polymer chains: 4
• Total formula weight: 80446.61

Authors

Liu, X.,Ma, J.,Zhang, H.,Feng, Y. (deposition date: 2016-08-08, release date: 2016-11-02, Last modification date: 2024-03-20)

Primary citation

Ma, J.,Zhang, X.,Feng, Y.,Zhang, H.,Wang, X.,Zheng, Y.,Qiao, W.,Liu, X.
Structural and Functional Study of Apoptosis-linked Gene-2Heme-binding Protein 2 Interactions in HIV-1 Production.
J. Biol. Chem., 291:26670-26685, 2016

PubMed Abstract: In the HIV-1 replication cycle, the endosomal sorting complex required for transport (ESCRT) machinery promotes viral budding and release in the late stages. In this process, the ESCRT proteins, ALIX and TSG101, are recruited through interactions with HIV-1 Gag p6. ALG-2, also known as PDCD6, interacts with both ALIX and TSG101 and bridges ESCRT-III and ESCRT-I. In this study, we show that ALG-2 affects HIV-1 production negatively at both the exogenous and endogenous levels. Through a yeast two-hybrid screen, we identified HEBP2 as the binding partner of ALG-2, and we solved the crystal structure of the ALG-2·HEBP2 complex. The function of ALG-2·HEBP2 complex in HIV-1 replication was further explored. ALG-2 inhibits HIV-1 production by affecting Gag expression and distribution, and HEBP2 might aid this process by tethering ALG-2 in the cytoplasm.

PubMed: 27784779
DOI: 10.1074/jbc.M116.752444

Experimental method

X-RAY DIFFRACTION (2.2 Å)