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Structure paper

TitleInvestigation of a Bicyclo[1.1.1]pentane as a Phenyl Replacement within an LpPLA2 Inhibitor.
Journal, issue, pagesACS Med Chem Lett, Vol. 8, Page 43-48, Year 2017
Publish dateAug 11, 2016 (structure data deposition date)
AuthorsMeasom, N.D. / Down, K.D. / Hirst, D.J. / Jamieson, C. / Manas, E.S. / Patel, V.K. / Somers, D.O.
External linksACS Med Chem Lett / PubMed:28105273
MethodsX-ray diffraction
Resolution1.91 Å
Structure data

PDB-5lp1:
CRYSTAL STRUCTURE OF HUMAN LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 IN COMPLEX WITH A [1.1.1]BICYCLOPENTANE-CONTAINING INHIBITOR AT 1.91A RESOLUTION.
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-71H:
~{N}-[2-(diethylamino)ethyl]-2-[2-[(4-fluorophenyl)methylsulfanyl]-4-oxidanylidene-5~{H}-cyclopenta[d]pyrimidin-1-yl]-~{N}-[[3-[4-(trifluoromethyl)phenyl]-1-bicyclo[1.1.1]pentanyl]methyl]ethanamide

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / PLASMA PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE / SECRETED PROTEIN / ALPHA/BETA-HYDROLASE-FOLD / LDL-BOUND; LIPOPROTEIN ASSOCIATED PHOSPHOLIPASE A2 / LP-PLA2 / GROUP VIIA PLA2 / GLYCOPROTEIN / HYDROLASE / LIPID DEGRADATION / POLYMORPHISM / SECRETED / HYDROLASE-HYDROLASE INHIBITOR COMPLEX

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