2KFH

Structure of the C-terminal domain of EHD1 with FNYESTGPFTAK

Summary for 2KFH

• Entry DOI: 10.2210/pdb2kfh/pdb
• Related: 2KFF 2KFG
• NMR Information: BMRB: 16181
• Descriptor: EH domain-containing protein 1, Rab11-FIP2 GPF peptide FNYESTGPFTAK, CALCIUM ION (3 entities in total)
• Functional Keywords: ehd1, calcium, cell membrane, coiled coil, endosome, membrane, nucleotide-binding, phosphoprotein, protein binding
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 13056.88

Authors

Kieken, F.,Jovic, M.,Tonelli, M.,Naslavsky, N.,Caplan, S.,Sorgen, P. (deposition date: 2009-02-20, release date: 2009-12-22, Last modification date: 2024-05-01)

Primary citation

Kieken, F.,Jovic, M.,Tonelli, M.,Naslavsky, N.,Caplan, S.,Sorgen, P.L.
Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.
Protein Sci., 18:2471-2479, 2009

PubMed Abstract: Eps15 homology (EH)-domain containing proteins are regulators of endocytic membrane trafficking. EH-domain binding to proteins containing the tripeptide NPF has been well characterized, but recent studies have shown that EH-domains are also able to interact with ligands containing DPF or GPF motifs. We demonstrate that the three motifs interact in a similar way with the EH-domain of EHD1, with the NPF motif having the highest affinity due to the presence of an intermolecular hydrogen bond. The weaker affinity for the DPF and GPF motifs suggests that if complex formation occurs in vivo, they may require high ligand concentrations, the presence of successive motifs and/or specific flanking residues.

PubMed: 19798736
DOI: 10.1002/pro.258

Experimental method

SOLUTION NMR