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1cj1
From Proteopedia
| 1cj1, resolution 3.00Å () | |||||||||
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| Ligands: | |||||||||
| Domains: | SH2 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN (HUMAN) COMPLEXED WITH A PHOSPHOTYROSYL DERIVATIVE
Previous efforts in the search for molecules capable of blocking the associations between the activated tyrosine kinase growth factor receptors and the SH2 domain of Grb2 had resulted in the identification of 3-amino-Z-pTyr-Ac6c-Asn-NH2, a high-affinity and selective antagonist of this SH2 domain. In the present paper, we report the successful replacement of asparagine in this compound by a beta-amino acid mimetic, which brings us closer to our objective of identifying a Grb2-SH2 antagonist suitable for pharmacological investigations.
Structure-based design, synthesis, and X-ray crystallography of a high-affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic., Furet P, Garcia-Echeverria C, Gay B, Schoepfer J, Zeller M, Rahuel J, J Med Chem. 1999 Jul 1;42(13):2358-63. PMID:10395476
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1CJ1 is a 12 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Furet P, Garcia-Echeverria C, Gay B, Schoepfer J, Zeller M, Rahuel J. Structure-based design, synthesis, and X-ray crystallography of a high-affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic. J Med Chem. 1999 Jul 1;42(13):2358-63. PMID:10395476 doi:10.1021/jm991013u
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