2JQ6
Structure of EH-domain of EHD1
2JQ6 の概要
| エントリーDOI | 10.2210/pdb2jq6/pdb |
| NMR情報 | BMRB: 15279 |
| 分子名称 | EH domain-containing protein 1, CALCIUM ION (2 entities in total) |
| 機能のキーワード | eh domain, ehd-1, metal binding protein |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15033.06 |
| 構造登録者 | Kieken, F.P.,Jovic, M.,Caplan, S.,Sorgen, P.L. (登録日: 2007-05-29, 公開日: 2008-04-15, 最終更新日: 2024-05-08) |
| 主引用文献 | Kieken, F.,Jovic, M.,Naslavsky, N.,Caplan, S.,Sorgen, P.L. EH domain of EHD1 J.Biomol.Nmr, 39:323-329, 2007 Cited by PubMed Abstract: EHD1 is a member of the mammalian C-terminal Eps15 homology domain (EH) containing protein family, and regulates the recycling of various receptors from the endocytic recycling compartment to the plasma membrane. The EH domain of EHD1 binds to proteins containing either an Asn-Pro-Phe or Asp-Pro-Phe motif, and plays an important role in the subcellular localization and function of EHD1. Thus far, the structures of five N-terminal EH domains from other proteins have been solved, but to date, the structure of the EH domains from the four C-terminal EHD family paralogs remains unknown. In this study, we have assigned the 133 C-terminal residues of EHD1, which includes the EH domain, and solved its solution structure. While the overall structure resembles that of the second of the three N-terminal Eps15 EH domains, potentially significant differences in surface charge and the structure of the tripeptide-binding pocket are discussed. PubMed: 17899392DOI: 10.1007/s10858-007-9196-0 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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