Structural Basis of Binding by Cyclic Nonphosphorylated Peptide Antagonists of Grb7 Implicated in Breast Cancer Progression

• Published in: Journal of molecular biology Vol. 412; no. 3; pp. 397 - 411
• Main Authors: Ambaye, Nigus D., Pero, Stephanie C., Gunzburg, Menachem J., Yap, MinYin, Clayton, Daniel J., Del Borgo, Mark P., Perlmutter, Patrick, Aguilar, Marie-Isabel, Shukla, Girja S., Peletskaya, Elena, Cookson, Michelle M., Krag, David N., Wilce, Matthew C.J., Wilce, Jacqueline A.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 23.09.2011
• Subjects: Amino Acid Sequence; amino acids; antagonists; antagonists & inhibitors; Antineoplastic Agents; Antineoplastic Agents - chemistry; Antineoplastic Agents - metabolism; bacteriophages; binding capacity; breast neoplasms; calorimetry; cell movement; chemistry; crystal structure; Crystallography, X-Ray; cyclic peptide; erbB-2 receptor; GRB7 Adaptor Protein; GRB7 Adaptor Protein - antagonists & inhibitors; GRB7 Adaptor Protein - chemistry; GRB7 Adaptor Protein - metabolism; Grb7 inhibitor; Humans; isolation & purification; ITC; Kinetics; metabolism; Models, Molecular; Molecular Sequence Data; Peptide Library; peptides; Peptides, Cyclic; Peptides, Cyclic - chemistry; Peptides, Cyclic - isolation & purification; Peptides, Cyclic - metabolism; phage display; Protein Binding; Protein Structure, Quaternary; Sequence Alignment; SH2 domain; titration; FAK; Grb7 inhibitor; SH2 domain; phage display; Grb; HRP; ITC; cyclic peptide; PDB

Growth-receptor-bound protein (Grb)7 is an adapter protein aberrantly overexpressed, along with the erbB-2 receptor in breast cancer and in other cancers. Normally recruited to focal adhesions with a role in cell migration, it is associated with erbB-2 in cancer cells and is found to exacerbate canc...