FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W59009676> ?p ?o ?g. }

• W59009676 endingPage "22778" @default.
• W59009676 startingPage "22770" @default.
• W59009676 abstract "As part of a structure-based drug design program directed against enzyme targets in the human immunodeficiency virus (HIV), we have determined the three-dimensional structures of the HIV type 1 protease complexed with two hydroxyethylene-based inhibitors. The inhibitors (SKF 107457 and SKF 108738) are hexapeptide substrate analogues with the scissile bond being replaced by a hydroxyethylene isostere. The structures were determined using x-ray diffraction data to 2.2 A measured at the Cornell High Energy Synchrotron Source on hexagonal crystals of each of the complexes. The structures have been extensively refined using a reciprocal space least-squares method to conventional crystallographic R factors of 0.186 and 0.159, respectively. The protein structure differs from that in the unliganded state of the enzyme and is most similar to that of the structure of the other reported (Jaskolski, M., Tomasselli, A. G., Sawyer, T. K., Staples, D. G., Heinrikson, R. L., Schneider, J., Kent, S. B. H., and Wlodawer, A. (1990) Biochemistry 29, 5889-5907) hydroxyethylene-based inhibitor complex. Unlike in that structure, however, the inhibitors are observed, in the present crystal structures, in two equally abundant orientations that are a consequence of the homodimeric nature of the enzyme coupled with the asymmetric structures of the inhibitors. Although the differences between the two inhibitors used in the present study are confined to the P1' site, the van der Waals interactions made by the inhibitor atoms with the amino acid residues in the protein differ throughout the structures of the inhibitors." @default.
• W59009676 created "2016-06-24" @default.
• W59009676 creator A5023674052 @default.
• W59009676 creator A5046832707 @default.
• W59009676 creator A5049868099 @default.
• W59009676 creator A5057510236 @default.
• W59009676 creator A5058805516 @default.
• W59009676 date "1994-05-31" @default.
• W59009676 modified "2023-09-28" @default.
• W59009676 title "The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations." @default.
• W59009676 cites W1608052268 @default.
• W59009676 cites W1637218542 @default.
• W59009676 cites W1642222223 @default.
• W59009676 cites W1878111742 @default.
• W59009676 cites W1965349185 @default.
• W59009676 cites W1974224443 @default.
• W59009676 cites W1985459186 @default.
• W59009676 cites W1986248827 @default.
• W59009676 cites W1989475707 @default.
• W59009676 cites W1995396220 @default.
• W59009676 cites W2006327082 @default.
• W59009676 cites W2013944709 @default.
• W59009676 cites W2014694459 @default.
• W59009676 cites W2028124297 @default.
• W59009676 cites W2036498783 @default.
• W59009676 cites W2039616336 @default.
• W59009676 cites W2048448899 @default.
• W59009676 cites W2056633621 @default.
• W59009676 cites W2060740730 @default.
• W59009676 cites W2066459154 @default.
• W59009676 cites W2069366448 @default.
• W59009676 cites W2077503061 @default.
• W59009676 cites W2085053424 @default.
• W59009676 cites W2085318243 @default.
• W59009676 cites W2087876594 @default.
• W59009676 cites W2097410498 @default.
• W59009676 cites W2099072469 @default.
• W59009676 cites W2117514600 @default.
• W59009676 cites W2160276605 @default.
• W59009676 cites W2165732545 @default.
• W59009676 cites W2211511465 @default.
• W59009676 cites W2034027861 @default.
• W59009676 doi "https://doi.org/10.2210/pdb1heg/pdb" @default.
• W59009676 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1429626" @default.
• W59009676 hasPublicationYear "1994" @default.
• W59009676 type Work @default.
• W59009676 sameAs 59009676 @default.
• W59009676 citedByCount "15" @default.
• W59009676 countsByYear W590096762018 @default.
• W59009676 countsByYear W590096762023 @default.
• W59009676 crossrefType "component" @default.
• W59009676 hasAuthorship W59009676A5023674052 @default.
• W59009676 hasAuthorship W59009676A5046832707 @default.
• W59009676 hasAuthorship W59009676A5049868099 @default.
• W59009676 hasAuthorship W59009676A5057510236 @default.
• W59009676 hasAuthorship W59009676A5058805516 @default.
• W59009676 hasConcept C115624301 @default.
• W59009676 hasConcept C126061179 @default.
• W59009676 hasConcept C178790620 @default.
• W59009676 hasConcept C180000673 @default.
• W59009676 hasConcept C181199279 @default.
• W59009676 hasConcept C185592680 @default.
• W59009676 hasConcept C2776714187 @default.
• W59009676 hasConcept C2776980637 @default.
• W59009676 hasConcept C2780120296 @default.
• W59009676 hasConcept C32909587 @default.
• W59009676 hasConcept C55493867 @default.
• W59009676 hasConcept C71240020 @default.
• W59009676 hasConcept C8010536 @default.
• W59009676 hasConcept C87282627 @default.
• W59009676 hasConceptScore W59009676C115624301 @default.
• W59009676 hasConceptScore W59009676C126061179 @default.
• W59009676 hasConceptScore W59009676C178790620 @default.
• W59009676 hasConceptScore W59009676C180000673 @default.
• W59009676 hasConceptScore W59009676C181199279 @default.
• W59009676 hasConceptScore W59009676C185592680 @default.
• W59009676 hasConceptScore W59009676C2776714187 @default.
• W59009676 hasConceptScore W59009676C2776980637 @default.
• W59009676 hasConceptScore W59009676C2780120296 @default.
• W59009676 hasConceptScore W59009676C32909587 @default.
• W59009676 hasConceptScore W59009676C55493867 @default.
• W59009676 hasConceptScore W59009676C71240020 @default.
• W59009676 hasConceptScore W59009676C8010536 @default.
• W59009676 hasConceptScore W59009676C87282627 @default.
• W59009676 hasIssue "32" @default.
• W59009676 hasLocation W590096761 @default.
• W59009676 hasOpenAccess W59009676 @default.
• W59009676 hasPrimaryLocation W590096761 @default.
• W59009676 hasRelatedWork W1637218542 @default.
• W59009676 hasRelatedWork W1802484108 @default.
• W59009676 hasRelatedWork W1965349185 @default.
• W59009676 hasRelatedWork W1966952510 @default.
• W59009676 hasRelatedWork W1974224443 @default.
• W59009676 hasRelatedWork W1985469117 @default.
• W59009676 hasRelatedWork W1986248827 @default.
• W59009676 hasRelatedWork W1989475707 @default.
• W59009676 hasRelatedWork W1995396220 @default.
• W59009676 hasRelatedWork W2026802618 @default.

• next