2q1j
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The discovery of glycine and related amino acid-based factor xa inhibitors
OverviewOverview
Herein, we report on the identification of three potent glycine and, related amino acid-based series of FXa inhibitors containing a neutral P1, chlorophenyl pharmacophore. A X-ray crystal structure has shown that, constrained glycine derivatives with optimized N-substitution can greatly, increase hydrophobic interactions in the FXa active site. Also, the, substitution of a pyridone ring for a phenylsulfone ring in the P4, sidechain resulted in an inhibitor with enhanced oral bioavailability.
About this StructureAbout this Structure
2Q1J is a Protein complex structure of sequences from Homo sapiens with and as ligands. Active as Coagulation factor Xa, with EC number 3.4.21.6 Full crystallographic information is available from OCA.
ReferenceReference
The discovery of glycine and related amino acid-based factor Xa inhibitors., Kohrt JT, Filipski KJ, Cody WL, Bigge CF, La F, Welch K, Dahring T, Bryant JW, Leonard D, Bolton G, Narasimhan L, Zhang E, Peterson JT, Haarer S, Sahasrabudhe V, Janiczek N, Desiraju S, Hena M, Fiakpui C, Saraswat N, Sharma R, Sun S, Maiti SN, Leadley R, Edmunds JJ, Bioorg Med Chem. 2006 Jul 1;14(13):4379-92. Epub 2006 Mar 10. PMID:16529937
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- Coagulation factor Xa
- Homo sapiens
- Protein complex
- Bigge, C.F.
- Cody, W.L.
- Filipski, K.J.
- Finzel, B.C.
- Kohrt, J.T.
- Zhang, E.
- CA
- FXI
- Blood coagulation
- Calcium
- Cleavage on pair of basic residues
- Coagulation fxa
- Egf-like domain
- Gamma-carboxyglutamic acid
- Glycoprotein
- Hydrolase
- Hydroxylation
- Polymorphism
- Protease
- Serine protease
- Zymogen