EIAV PROTEASE COMPLEXED WITH AN INHIBITOR LP-130
4-[2-(2-ACETYLAMINO-3-NAPHTALEN-1-YL-PROPIONYLAMINO)-4-METHYL-PENTANOYLAMINO]-3-HYDROXY-6-METHYL-HEPTANOIC ACID [1-(1-CARBAMOYL-2-NAPHTHALEN-1-YL-ETHYLCARBAMOYL)-PROPYL]-AMIDE
Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
VTYNLEKRPTTIVLINDTPLNVLLDTGADTSVLTTAHYNRLKYRGRKYQGTGIGGVGGNVETFSTPVTIKKKGRHIKTRM LVADIPVTILGRDILQDLGAKLVL
THIS FILE CONTAINS ONLY A MONOMER, WHILE THE ACTIVE ENZYME IS A DIMER. IN ORDER TO CREATE A DIMERIC MOLECULE, CRYSTALLOGRAPHIC COORDINATES NEED TO BE TRANSFORMED TO (-X), Y, (-Z). THE TWO ORIENTATIONS OF THE INHIBITOR CREATED IN THAT MANNER OVERLAP, WITH COMPLETE SUPERPOSITION AT THE PERIPHERY AND SOME DEVIATION IN THE CENTER. RESIDUES 56 - 58 HAVE BEEN MODELED WITH TWO ORIENTATIONS OF THEIR MAIN CHAINS, SINCE THEY FORM ALTERNATE HYDROGEN BONDS, DUE TO THE SAME DISORDER PHENOMENON.
ASPARTIC PROTEASE, RETROPEPSIN, RETROVIRUS, EIAV, HORSE
RSERNKKGIQCQGEGSSRGSQPGQFVGVTYNLEKRPTTIVLINDTPLNVLLDTGADTSVLTTAHYNRLKYRGRKYQGTGI IGVGGNVETFSTPVTIKKKGRHIKTRMLVADIPVTILGRDILQDLGAKLVLAQLSKEIKFRKIELKEGTMGPKIPQWPLT KEKLEGAKEIVQRLLSEGKISEASDNNPYNSPIFVIKKKSGKWRLLQDL