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CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A TETRAHYDROISOQUINOLINE INHIBITORCRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A TETRAHYDROISOQUINOLINE INHIBITOR
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe co-crystal structure of beta-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. This finding provided the basis for a general hypothesis of a reverse binding mode for beta-phenethylamine-based DPP-IV inhibitors. Novel inhibitor design concepts that obviate substrate-like structure-activity relationships (SAR) were thereby enabled, and novel, potent inhibitors were discovered. The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors.,Nordhoff S, Cerezo-Galvez S, Feurer A, Hill O, Matassa VG, Metz G, Rummey C, Thiemann M, Edwards PJ Bioorg Med Chem Lett. 2006 Mar 15;16(6):1744-8. Epub 2006 Jan 11. PMID:16376544[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- Dipeptidyl-peptidase IV
- Sus scrofa
- Cerezo-Galvez, S.
- Edwards, P J.
- Feurer, A.
- Hill, O.
- Matassa, V G.
- Metz, G.
- Nordhoff, S.
- Rummey, C.
- Thiemann, M.
- Aminopeptidase
- Complex
- Diabetes mellitus
- Dpp-iv
- Drug design
- Glycoprotein
- Hydrolase
- Hydrolase-inhibitor complex
- Hydrolase/inhibitor
- Protease
- Serine protease
- Signal-anchor
- Transmembrane