3HLO: Crystal Structure Of Chemically Synthesized 'covalent Dimer' [gly51D- Ala51']hiv-1 Protease

We have used chemical protein synthesis and advanced physical methods to probe dynamics-function correlations for the HIV-1 protease, an enzyme that has received considerable attention as a target for the treatment of AIDS. Chemical synthesis was used to prepare a series of unique analogues of the HIV-1 protease in which the flexibility of the "flap" structures (residues 37-61 in each monomer of the homodimeric protein molecule) was systematically varied. These analogue enzymes were further studied by X-ray crystallography, NMR relaxation, and pulse-EPR methods, in conjunction with molecular dynamics simulations. We show that conformational isomerization in the flaps is correlated with structural reorganization of residues in the active site, and that it is preorganization of the active site that is a rate-limiting factor in catalysis.
PDB ID: 3HLODownload
MMDB ID: 93137
PDB Deposition Date: 2009/5/27
Updated in MMDB: 2011/08
Experimental Method:
x-ray diffraction
Resolution: 1.6  Å
Similar Structures:
Biological Unit for 3HLO: monomeric; determined by author and by software (PISA)
Molecular Components in 3HLO
Label Count Molecule
Protein (1 molecule)
'covalent Dimer' [gly51/d-ala51'] Hiv-1 Protease
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB