Immunodeficiency virus protease
From Proteopedia
| |||||||||
| 2nmz, resolution 0.97Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||||
| Gene: | gag (Human immunodeficiency virus 1) | ||||||||
| Activity: | HIV-1 retropepsin, with EC number 3.4.23.16 | ||||||||
| Related: | 2nmw, 2nmy, 2nnk, 2nnp | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
HIV is a notoriously lethal virus that is known to cause AIDS. There currently is no cure or vaccine. But, scientists have discovered treatments that can slow progression of the HIV virus, thanks in large part to our understanding of the structure of HIV-1 protease, seen here on the right in complex with a potent drug used for slowing the progression of HIV, (PDB code: 2nmz).
HIV-1 protease is a protein made by the HIV virus that is crucial to the virus's infectious capacity. The virus makes certain proteins that need to be cleaved, or cut, in order to transform into mature, fully-functional proteins that can allow the virus to infect new cells. HIV-1 protease is responsible for cleaving these nascent proteins into their mature form.
Looking at the structure of HIV-1 protease, we see that the protein is composed of , shown here in cartoon backbone representation to highlight secondary structure. Each subunit consists of the same small chain of only 99 amino acids. The subunits come together in such as way as to , shown here in spacefilling representation to showcase the physical surface of the protein. The protein to-be-cleaved sits in this tunnel. In the middle of the tunnel is the of the protease: (residue numbers 25, 26, and 27 on one chain and 125, 126, and 127 on the second) with acting as the catalytic residues.
Saquinavir was the the first FDA approved protease inhibitor.
(large scene, takes a while to load) to allow proteins to enter the tunnel.
PAGE IN PROGRESS Eran Hodis 19:10, 15 August 2008 (IDT)
References
- Atomic resolution crystal structures of HIV-1 protease and mutants V82A and I84V with saquinavir., Tie Y, Kovalevsky AY, Boross P, Wang YF, Ghosh AK, Tozser J, Harrison RW, Weber IT, Proteins. 2007 Apr 1;67(1):232-42. PMID:17243183
- The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU., Spinelli S, Liu QZ, Alzari PM, Hirel PH, Poljak RJ, Biochimie. 1991 Nov;73(11):1391-6. PMID:1799632
Links
- HIV-1 Protease featured in David S. Goodsell's Molecule of the Month
- HIV-1 Protease in Wikipedia
This page is not a fully developed page, but was created as an example for the press release of the Proteopedia article in the open-access journal Genome Biology. Please expand this page with additional information and references.
Proteopedia Page Contributors and Editors (what is this?)
Joel L. Sussman, Michal Harel, Eran Hodis, Mark Hoelzer, David Canner, Eric Martz, Ann Taylor, Wayne Decatur, Alexander Berchansky, Jaime Prilusky, Karsten Theis
