Evidence map›Paper›PMID 26460595›Full record

ArticleThe FEBS journal2016

Design of composite inhibitors targeting glutamate carboxypeptidase II: the importance of effector functionalities.

Zora Novakova, Jiri Cerny, Cindy J Choy, Jessie R Nedrow, Joeseph K Choi, Jacek Lubkowski, Clifford E Berkman, Cyril Barinka

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  10. Building and rebuilding N-glycans in protein structure models.Acta crystallographica. Section D, Structural biology · 2019
    Article
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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

8 authors at 3 institutions in 2 countries.

Zora NovakovaInstitute of Biotechnology, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Jiri CernyInstitute of Biotechnology, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Cindy J ChoyDepartment of Chemistry, Washington State University, Pullman, WA, USA.
Jessie R NedrowDepartment of Chemistry, Washington State University, Pullman, WA, USA.
Joeseph K ChoiDepartment of Chemistry, Washington State University, Pullman, WA, USA.
Jacek LubkowskiNational Cancer Institute, Center for Cancer Research, Macromolecular Crystallography Laboratory, Frederick, MD, USA.
Clifford E BerkmanDepartment of Chemistry, Washington State University, Pullman, WA, USA.
Cyril BarinkaInstitute of Biotechnology, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Washington State University · USCzech Academy of Sciences, Institute of Biotechnology · CZNational Institutes of Health · US

Funding

Probe Optimization for Prostate Cancer DetectionR01CA140617 · NCI · WASHINGTON STATE UNIVERSITY · PI BERKMAN, CLIFFORD · 2010 to 2013
$1.8M
NCI NIH HHS R01 CA140617
6 · The paper itself

Abstract

Inhibitors targeting human glutamate carboxypeptidase II (GCPII) typically consist of a P1' glutamate-derived binding module, which warrants the high affinity and specificity, linked to an effector function that is positioned within the entrance funnel of the enzyme. Here we present a comprehensive structural and computational study aimed at dissecting the importance of the effector function for GCPII binding and affinity. To this end we determined crystal structures of human GCPII in complex with a series of phosphoramidate-based inhibitors harboring effector functions of diverse physicochemical characteristics. Our data show that higher binding affinities of phosphoramidates, compared to matching phosphonates, are linked to the presence of additional hydrogen bonds between Glu424 and Gly518 of the enzyme and the amide group of the phosphoramidate. While the positioning of the P1' glutamate-derived module within the S1' pocket of GCPII is invariant, interaction interfaces between effector functions and residues lining the entrance funnel are highly varied, with the positively charged arginine patch defined by Arg463, Arg534 and Arg536 being the only 'hot-spot' common to several studied complexes. This variability stems in part from the fact that the effector/GCPII interfaces generally encompass isolated areas of nonpolar residues within the entrance funnel and resulting van der Waals contacts lack the directionality typical for hydrogen bonding interactions. The presented data unravel a complexity of binding modes of inhibitors within non-prime site(s) of GCPII and can be exploited for the design of novel GCPII-specific compounds. PDB ID CODES: Atomic coordinates of the present structures together with the experimental structure factor amplitudes were deposited at the RCSB Protein Data Bank under accession codes 4P44 (complex with JRB-4-81), 4P45 (complex with JRB-4-73), 4P4B (complex with CTT54), 4P4D (complex with MP1C), 4P4E (complex with MP1D), 4P4F (complex with NC-2-40), 4P4I (complex with T33) and 4P4J (complex with T33D).

Indexed as

Drug DesignAmidesAntigens, SurfaceCrystallography, X-RayDose-Response Relationship, DrugEnzyme InhibitorsGlutamate Carboxypeptidase IIHumansHydrogen BondingModels, MolecularMolecular StructurePhosphoric AcidsStructure-Activity RelationshipAmidesAntigens, SurfaceEnzyme InhibitorsFOLH1 protein, humanGlutamate Carboxypeptidase IIphosphoramidic acidPhosphoric Acidsmolecular modelingNAALADasephosphoramidateprostate-specific membrane antigenX-ray crystallography

Identifiers

PMID26460595
PMCPMC4712110
OpenAlexW2125994882

What OpenQuestion holds

Textmetadata
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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.