2KFH
Structure of the C-terminal domain of EHD1 with FNYESTGPFTAK
2KFH の概要
エントリーDOI | 10.2210/pdb2kfh/pdb |
関連するPDBエントリー | 2KFF 2KFG |
NMR情報 | BMRB: 16181 |
分子名称 | EH domain-containing protein 1, Rab11-FIP2 GPF peptide FNYESTGPFTAK, CALCIUM ION (3 entities in total) |
機能のキーワード | ehd1, calcium, cell membrane, coiled coil, endosome, membrane, nucleotide-binding, phosphoprotein, protein binding |
由来する生物種 | Homo sapiens (human) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 13056.88 |
構造登録者 | Kieken, F.,Jovic, M.,Tonelli, M.,Naslavsky, N.,Caplan, S.,Sorgen, P. (登録日: 2009-02-20, 公開日: 2009-12-22, 最終更新日: 2024-05-01) |
主引用文献 | 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 Cited by 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: 19798736DOI: 10.1002/pro.258 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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