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PDBsum entry 4g1f
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Hydrolase/hydrolase inhibitor
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PDB id
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4g1f
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PDB id:
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| Name: |
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Hydrolase/hydrolase inhibitor
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Title:
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Crystal structure of human dipeptidyl peptidase iv in complex with a pyridopyrimidinedione analogue
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Structure:
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Dipeptidyl peptidase 4. Chain: a, b, c, d. Fragment: unp residues 39-766. Synonym: adabp, adenosine deaminase complexing protein 2, adcp-2, dipeptidyl peptidase iv, dpp iv, t-cell activation antigen cd26, tp103, dipeptidyl peptidase 4 membrane form, dipeptidyl peptidase iv membrane form, dipeptidyl peptidase 4 soluble form, dipeptidyl peptidase iv soluble form. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: adcp2, cd26, dpp4. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108
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Resolution:
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2.90Å
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R-factor:
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0.209
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R-free:
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0.259
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Authors:
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R.J.Skene,S.L.Gwaltney
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Key ref:
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B.Lam
et al.
(2012).
Structure-based design of pyridopyrimidinediones as dipeptidyl peptidase IV inhibitors.
Bioorg Med Chem Lett,
22,
6628-6631.
PubMed id:
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Date:
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10-Jul-12
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Release date:
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27-Feb-13
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PROCHECK
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Headers
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References
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P27487
(DPP4_HUMAN) -
Dipeptidyl peptidase 4 from Homo sapiens
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Seq:
Struc:
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766 a.a.
724 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.4.14.5
- dipeptidyl-peptidase Iv.
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Reaction:
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Release of an N-terminal dipeptide, Xaa-Xbb-|-Xcc, from a polypeptide, preferentially when Xbb is Pro, provided Xcc is neither Pro nor hydroxyproline.
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Bioorg Med Chem Lett
22:6628-6631
(2012)
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PubMed id:
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Structure-based design of pyridopyrimidinediones as dipeptidyl peptidase IV inhibitors.
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B.Lam,
Z.Zhang,
J.A.Stafford,
R.J.Skene,
L.Shi,
S.L.Gwaltney.
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ABSTRACT
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Dipeptidyl peptidase IV (DPP-4) inhibitors have been shown to enhance GLP-1
levels and thereby improve hyperglycemia in type II diabetes. From a small
fragment hit, using structure-based design, we have discovered a new class of
non-covalent, potent and selective DPP-4 inhibitors.
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Links
