Peptide

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(Ace)(Slz)(Ptr)Vnvp

Basic information

CPKB ID CP02724
Source

Synthetic construct [Division : Synthetic]

Wikipedia: Synthetic construct

DPL2  

Information

cyclic phosphopeptides containing nonreducible mimics of cystine were synthesized that show high affinity and specificity toward the Src homology (SH2) domain of the growth factor receptor-binding protein (Grb2). Replacement of the cystine in the cyclic heptapeptide cyclo(CYVNVPC) by D-alpha-acetylthialysine or D-alpha-lysine gave cyclo(YVNVP(D-alpha-acetyl-thiaK)) (22) and cyclo(YVNVP(D-alpha-acetyl-K)) (30), which showed improved binding 10-fold relative to that of the control peptide KPFYVNVEF (1).

DPL2|DPL_553  

Legend

Sequence

Local alignment
One-letter code

(ACE)(SLZ)(PTR)VNVP

DPL2|DPL_553

Binding Target

Detail

Uniprot:  P62993

Kind:  Protein>Protein domain

Organism:  Homo sapiens(Human)

Evidevce:  DPL2   DPL2

Sequence:  MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV

General Function:

      Sh3/sh2 adaptor activity

Specific Function:

      The growth factor receptor-binding (Grb2) adaptor protein plays a central role in signaling by receptor tyrosine kinases. Grb2 is necessary for activation of the Ras pathway via complex formation with the Ras exchange factor Sos. 2 The Src homology (SH2) domain of Grb2 binds preferentially to phosphotyrosines (Y*s) with the sequence motif Y*XNX. The two SH3 domains of Grb2 bind to Sos, which catalyzes GTP/GDP exchange on Ras, thereby activating the GTPase and downstream kinase cascade.

Additional database information: TTD[SH2 domain of Grb2(1)]

Manufacturers

Manufacturers Name Value
CreativePeptides
Bayer healthcare pharmaceuticals
Upsher smith laboratories
Merck
Manufacturers Name Value
Apotex
Baxter Healthcare Corp
Pharmasources
Novartis
AstraZeneca

Forecasting tools

Forecasting tools Value
Sequence to Structure
(ACE)(SLZ)(PTR)VNVP
Sequence Properties
(ACE)(SLZ)(PTR)VNVP
Expasy ProtParam Tool (ACE)(SLZ)(PTR)VNVP
SEA RUN SEA Predictions

Information Source

Property Name Property ID
Drugbank
DPL2 DPL_553
DRAMP3
Uniprot
Cybase
CONOSERVER
CHEMBL
CTD
Wikipedia
KEGG Compound/Drug
EPA DSSTox
FDA Global Substance Registration System (GSRS)
DTP/NCI

Reference

Pubmed_ID Title DOI Journal

1446006

 Structures of three new homotyrosine-containing microcystins and a new homophenylalanine variant from Anabaena sp. strain 66 10.1021/tx00029a011.

Chem Res Toxicol

Structures of three new homotyrosine-containing microcystins and a new homophenylalanine variant from Anabaena sp. strain 66

Abstract

  • A hepatotoxic strain of cyanobacterium Anabaena sp. 66 was isolated from a hepatotoxic water bloom sample in Lake Kiikkara, Finland. Four cyclic heptapeptide hepatotoxins were isolated and purified by HPLC from cultured cells of this organism. The structures of three new homotyrosine (Hty) containing toxins, Dha7microcystin-HtyR (Dha = dehydroalanine) (1), D-Asp3,Dha7microcystin-HtyR (2), and L-Ser7microcystin-HtyR (3), were assigned, based upon amino acid analyses using both a Waters Pico Tag HPLC system and chiral capillary GC, 1H NMR, fast atom bombardment mass spectrometry (FABMS), and collisionally induced tandem FABMS. A new homophenylalanine (Hph) variant of 1, Dha7microcystin-HphR (4), was also obtained as a minor component. Compound 3 is most likely a biosynthetic precursor of 1. The four new toxins did not have an N-methyl group at the dehydroamino acid or its precursor unit.