(R)-PFI-2

(R)-PFI-2 : inhibitor of SETD7

Structure

SERP Rating

In Cells

(3 ratings)

In Model Organisms

(0 ratings)

note: The Chemical Probes Portal only endorses compounds as chemical probes for use as specific and selective modulators of the proposed target if they receive three or more (3-4) stars.

Information

SETD7

Inhibitor

100 nM - 5 uM

DOI - 10.1073/pnas.1407358111

Probe Availability:

In Vitro Validations

Uniprot ID: Q8WTS6

Target Class: Epigenetic

Target SubClass: Protein methyltransferase

Potency: Ki (app)

Potency Value: 0.33 nM

Potency Assay: IC50 = 2 nM in radioactive methyltransferase assay, transfer of 3H from 3H-SAM to peptide substrate

PDB ID for probe-target interaction (3D structure): 4JLG

Target aliases:

Histone-lysine N-methyltransferase SETD7, SET9, SE ...

DOI Reference: 10.1073/pnas.1407358111

In Cell Validations

In Vivo Data

No in Vivo Validations

Off-Target Selectivity Assesments

Potency assay (off target): 1000-fold selective compared with 18 other protein methyltransferases and DNMT

Probe Selectivity in Vitro:

No notable activity against 134 targets (ion channels, GPCRs, or other enzymes) up to 10 uM.

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SERP ratings and comments

SERP Ratings

In Cell Rating

(last updated: 17 May 2016 )

SERP Ratings

In Cell Rating

SERP Comments:

The enantiomer (S)-PFI-2 is 500-fold less active, making it a useful negative control. Note, the probe also has an unusual cofactor-dependent mechanism of action: (R)-PFI-2 binds to SETD7 only in the presence of SAM; inhibition of SETD7 activity by (R)-PFI-2 is unlikely to be purely substrate-competitive in the classical sense.

(last updated: 18 May 2016 )

SERP Ratings

In Cell Rating

SERP Comments:

This is currently the most potent probe available for this target. The availability of the negative control compound further strengthens the usability of this inhibitor.

(last updated: 6 Jun 2016 )