1BXX
MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH TGN38 INTERNALIZATION PEPTIDE DYQRLN
1BXX の概要
| エントリーDOI | 10.2210/pdb1bxx/pdb |
| 分子名称 | PROTEIN (AP50), PROTEIN (TGN38 PEPTIDE) (3 entities in total) |
| 機能のキーワード | endocytosis, adaptor, peptide complex, endocytosis-exocytosis complex, endocytosis/exocytosis |
| 由来する生物種 | Rattus norvegicus (Norway rat) 詳細 |
| 細胞内の位置 | Cell membrane : P84092 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 33567.22 |
| 構造登録者 | |
| 主引用文献 | Owen, D.J.,Evans, P.R. A structural explanation for the recognition of tyrosine-based endocytotic signals. Science, 282:1327-1332, 1998 Cited by PubMed Abstract: Many cell surface proteins are marked for endocytosis by a cytoplasmic sequence motif, tyrosine-X-X-(hydrophobic residue), that is recognized by the mu2 subunit of AP2 adaptors. Crystal structures of the internalization signal binding domain of mu2 complexed with the internalization signal peptides of epidermal growth factor receptor and the trans-Golgi network protein TGN38 have been determined at 2.7 angstrom resolution. The signal peptides adopted an extended conformation rather than the expected tight turn. Specificity was conferred by hydrophobic pockets that bind the tyrosine and leucine in the peptide. In the crystal, the protein forms dimers that could increase the strength and specificity of binding to dimeric receptors. PubMed: 9812899DOI: 10.1126/science.282.5392.1327 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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