Crystal structures of a high-affinity macrocyclic peptide bound to the Grb2 SH2 cancer signaling domain revealed precise binding interactions, guiding further optimization of this anticancer peptide drug approach.
Key findingX-ray crystal structures of a high-affinity macrocyclic peptide mimetic bound to Grb2 SH2 domain revealed specific hydrogen bonds and hydrophobic cont
What the researchers found
X-ray crystal structures of a high-affinity macrocyclic peptide mimetic bound to Grb2 SH2 domain revealed specific hydrogen bonds and hydrophobic contacts driving picomolar binding — providing the structural blueprint for optimizing this cancer drug scaffold.
Why it matters
Relevant for cyclic-peptides, cancer, peptide-design.
How the study worked
in-vitro study on cyclic-peptides, cancer.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2005.
The bigger picture
Advances peptide research with clinical implications.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain.
Journal of molecular biology, 353(1), 104-15
Citation
Phan, Jason; Shi, Zhen-Dan; Burke, Terrence R; Waugh, David S. (2005). Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain.. Journal of molecular biology, 353(1), 104-15.