Literature summary for 3.4.23.B8 extracted from

Selvaraj, C.; Singh, P.; Singh, S.K.
Molecular insights on analogs of HIV PR inhibitors toward HTLV-1 PR through QM/MM interactions and molecular dynamics studies: comparative structure analysis of wild and mutant HTLV-1 PR (2014), J. Mol. Recognit., 27, 696-706.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
sequence and structural alignments of HTLV-1 protease and HIV-1 protease. 95% of ligand recognizing active site amino acids are common in both receptors, the approved drugs of HIV proteases are unable to function as HTLV-1 protease inhibitors. The reported amino acid Asp30 from HIV-1 proease is substituted as Met37 in HTLV protease. Met37 is playing the vital role in ejection of HIV protease inhibitors from the binding pocket of HTLV protease	Human T-cell leukemia virus type I

Crystallization (Comment)

Organism

sequence and structural alignments of HTLV-1 protease and HIV-1 protease. 95% of ligand recognizing active site amino acids are common in both receptors, the approved drugs of HIV proteases are unable to function as HTLV-1 protease inhibitors. The reported amino acid Asp30 from HIV-1 proease is substituted as Met37 in HTLV protease. Met37 is playing the vital role in ejection of HIV protease inhibitors from the binding pocket of HTLV protease

Human T-cell leukemia virus type I

Protein Variants

Protein Variants	Comment	Organism
M37D	mutation introduced to mimick HIV protease inhibitor binding site. Met37 is playing the vital role in ejection of HIV protease inhibitors from the binding pocket of HTLV protease	Human T-cell leukemia virus type I

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	design of inhibitory compounds that circumvent the dominant residue Met37 in the binding pocket	Human T-cell leukemia virus type I

Organism

Organism	UniProt	Comment	Textmining
Human T-cell leukemia virus type I	P03362	Gag-Pol polyprotein	-

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Release 2023.1 (January 2023)