Evidence map›Paper›PMID 12690074›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism.

Michael Engel, Torsten Hoffmann, Leona Wagner, Michael Wermann, Ulrich Heiser, Reiner Kiefersauer, Robert Huber, Wolfram Bode, Hans-Ulrich Demuth, Hans Brandstetter

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
10.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

90 citing papers in PubMed, 304 citations in OpenAlex.

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  9. Review
  10. Computational Modeling of the Interactions between DPP IV and Hemorphins.International journal of molecular sciences · 2024
    Article
  11. Review
  12. Review
  13. Article
  14. Depletion of polyfunctional CD26Experimental hematology & oncology · 2023
    Article
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30 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Michael EngelMax-Planck-Institut für Biochemie, Abt. Strukturforschung, D-82152 Martinsried, Germany.
Torsten Hoffmann
Leona Wagner
Michael Wermann
Ulrich Heiser
Reiner Kiefersauer
Robert Huber
Wolfram Bode
Hans-Ulrich Demuth
Hans Brandstetter
Max Planck Institute of Biochemistry · DEProbiodrug (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The membrane-bound glycoprotein dipeptidyl peptidase IV (DP IV, CD26) is a unique multifunctional protein, acting as receptor, binding and proteolytic molecule. We have determined the sequence and 1.8 A crystal structure of native DP IV prepared from porcine kidney. The crystal structure reveals a 2-2-2 symmetric tetrameric assembly which depends on the natively glycosylated beta-propeller blade IV. The crystal structure indicates that tetramerization of DP IV is a key mechanism to regulate its interaction with other components. Each subunit comprises two structural domains, the N-terminal eight-bladed beta-propeller with open Velcro topology and the C-terminal alpha/beta-hydrolase domain. Analogy with the structurally related POP and tricorn protease suggests that substrates access the buried active site through the beta-propeller tunnel while products leave the active site through a separate side exit. A dipeptide mimicking inhibitor complexed to the active site discloses key determinants for substrate recognition, including a Glu-Glu motif that distinguishes DP IV as an aminopeptidase and an oxyanion trap that binds and activates the P(2)-carbonyl oxygen necessary for efficient postproline cleavage. We discuss active and nonactive site-directed inhibition strategies of this pharmaceutical target protein.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCatalysisCrystallography, X-RayDipeptidyl Peptidase 4DNA, ComplementaryMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtease InhibitorsProtein ConformationSequence Homology, Amino AcidSwineDipeptidyl Peptidase 4DNA, ComplementaryProtease Inhibitors

Identifiers

PMID12690074
PMCPMC154298
OpenAlexW2155060077

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.