2bub: Difference between revisions
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|PDB= 2bub |SIZE=350|CAPTION= <scene name='initialview01'>2bub</scene>, resolution 2.66Å | |PDB= 2bub |SIZE=350|CAPTION= <scene name='initialview01'>2bub</scene>, resolution 2.66Å | ||
|SITE= <scene name='pdbsite=AC1:Fpb+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fpb+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=FPB:N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE'>FPB</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bub OCA], [http://www.ebi.ac.uk/pdbsum/2bub PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bub RCSB]</span> | |||
}} | }} | ||
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[[Category: Rummey, C.]] | [[Category: Rummey, C.]] | ||
[[Category: Thiemann, M.]] | [[Category: Thiemann, M.]] | ||
[[Category: aminopeptidase]] | [[Category: aminopeptidase]] | ||
[[Category: complex]] | [[Category: complex]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:11:51 2008'' | ||
Revision as of 02:11, 31 March 2008
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| , resolution 2.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Dipeptidyl-peptidase IV, with EC number 3.4.14.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A REVERSED AMIDE INHIBITOR
OverviewOverview
The 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.
About this StructureAbout this Structure
2BUB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Dipeptidyl-peptidase IV
- Homo sapiens
- Single protein
- 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
- Protease
- Serine protease
- Signal-anchor
- Transmembrane