6CB0

Crystal Structure of the FAK FERM domain

Summary for 6CB0

• Entry DOI: 10.2210/pdb6cb0/pdb
• Descriptor: Focal adhesion kinase 1 (2 entities in total)
• Functional Keywords: fak ferm domain, src sh3 binding site, transferase
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 2
• Total formula weight: 86580.29

Authors

Dementiev, A.,Marlowe, T. (deposition date: 2018-02-01, release date: 2019-02-06, Last modification date: 2023-10-04)

Primary citation

Marlowe, T.,Dementiev, A.,Figel, S.,Rivera, A.,Flavin, M.,Cance, W.
High resolution crystal structure of the FAK FERM domain reveals new insights on the Druggability of tyrosine 397 and the Src SH3 binding site.
BMC Mol Cell Biol, 20:10-10, 2019

PubMed Abstract: Focal Adhesion Kinase (FAK) is a major cancer drug target that is involved in numerous aspects of tumor progression and survival. While multiple research groups have developed ATP-competitive small molecule inhibitors that target the kinase enzyme, recent attention has been focused on the FAK FERM (Band 4.1, Ezrin, Radixin, Moesin) domain that contains key residue Y397 and contributes to many protein-protein interactions. Previous x-ray crystal structures of the FAK FERM domain gave conflicting results on the structure of the Y397 region and therefore the overall druggability.

PubMed: 31109284
DOI: 10.1186/s12860-019-0193-4

Experimental method

X-RAY DIFFRACTION (1.97 Å)