2VYI

Crystal Structure of the TPR domain of Human SGT

Summary for 2VYI

• Entry DOI: 10.2210/pdb2vyi/pdb
• Descriptor: SGTA PROTEIN (2 entities in total)
• Functional Keywords: sgt, chaperone, tpr repeat, phosphoprotein, tetratricopeptide repeat protein, host-virus interaction
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 28860.35

Authors

Dutta, S.,Tan, Y.J. (deposition date: 2008-07-24, release date: 2008-08-12, Last modification date: 2024-10-16)

Primary citation

Dutta, S.,Tan, Y.J.
Structural and Functional Characterization of Human Sgt and its Interaction with Vpu of the Human Immunodeficiency Virus Type 1.
Biochemistry, 47:10123-, 2008

PubMed Abstract: The small glutamine-rich tetratricopeptide repeat protein (SGT) belongs to a family of cochaperones that interacts with both Hsp70 and Hsp90 via the so-called TPR domain. Here, we present the crystal structure of the TPR domain of human SGT (SGT-TPR), which shows that it contains typical features found in the structures of other TPR domains. Previous studies show that full-length SGT can bind to both Vpu and Gag of human immunodeficiency virus type 1 (HIV-1) and the overexpression of SGT in cells reduces the efficiency of HIV-1 particle release. We show that SGT-TPR can bind Vpu and reduce the amount of HIV-1 p24, which is the viral capsid, secreted from cells transfected with the HIV-1 proviral construct, albeit at a lower efficiency than full-length SGT. This indicates that the TPR domain of SGT is sufficient for the inhibition of HIV-1 particle release but the N- and/or C-terminus also have some contributions. The SGT binding site in Vpu was also identified by using peptide array and confirmed by GST pull-down assay.

PubMed: 18759457
DOI: 10.1021/BI800758A

Experimental method

X-RAY DIFFRACTION (2.4 Å)