2MYQ

NMR structure of an Odin-Sam1 fragment

Summary for 2MYQ

• Entry DOI: 10.2210/pdb2myq/pdb
• NMR Information: BMRB: 25458
• Descriptor: Ankyrin repeat and SAM domain-containing protein 1A (1 entity in total)
• Functional Keywords: signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q92625
• Total number of polymer chains: 1
• Total formula weight: 4965.63

Authors

Mercurio, F.A.,Leone, M. (deposition date: 2015-01-30, release date: 2015-07-08, Last modification date: 2024-11-20)

Primary citation

Mercurio, F.A.,Di Natale, C.,Pirone, L.,Scognamiglio, P.L.,Marasco, D.,Pedone, E.M.,Saviano, M.,Leone, M.
Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam.
Chembiochem, 16:1629-1636, 2015

PubMed Abstract: Odin is a protein belonging to the ANKS family, and has two tandem Sam domains. The first, Odin-Sam1, binds to the Sam domain of the EphA2 receptor (EphA2-Sam); this interaction could be crucial for the regulation of receptor endocytosis and might have an impact on cancer. Odin-Sam1 associates with EphA2-Sam by adopting a "mid-loop/end-helix" model. In this study three peptide sequences, encompassing the mid-loop interacting portion of Odin-Sam1 and its C-terminal α5 helix, were designed. Their conformational properties were analyzed by CD and NMR. In addition, their abilities to interact with EphA2-Sam were investigated by SPR studies. The peptides adopt a predominantly disordered state in aqueous buffer, but a higher helical content is evident in the presence of the cosolvent trifluoroethanol. Dissociation constants towards EphA2-Sam were in the high micromolar range. The structural findings suggest further routes for the design of potential anti-cancer therapeutics as inhibitors of EphA2-Sam heterotypic interactions.

PubMed: 26120079
DOI: 10.1002/cbic.201500197

Experimental method

SOLUTION NMR