2VX8
Vamp7 longin domain Hrb peptide complex
2VX8 の概要
| エントリーDOI | 10.2210/pdb2vx8/pdb |
| 分子名称 | NUCLEOPORIN-LIKE PROTEIN RIP, VESICLE-ASSOCIATED MEMBRANE PROTEIN 7, CHLORIDE ION (3 entities in total) |
| 機能のキーワード | endocytosis, exocytosis, membrane protein, signal-anchor, snare, membrane, endosome, lysosome, transport, cytoplasmic vesicle, endoplasmic reticulum, protein transport, vesicle transport, transmembrane, golgi apparatus, clathrin adaptor |
| 由来する生物種 | HOMO SAPIENS (HUMAN) 詳細 |
| 細胞内の位置 | Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein: P70280 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 74830.45 |
| 構造登録者 | |
| 主引用文献 | Pryor, P.R.,Jackson, L.,Gray, S.R.,Edeling, M.A.,Thompson, A.,Sanderson, C.M.,Evans, P.R.,Owen, D.J.,Luzio, J.P. Molecular Basis for the Sorting of the Snare Vamp7 Into Endocytic Clathrin-Coated Vesicles by the Arfgap Hrb. Cell(Cambridge,Mass.), 134:817-, 2008 Cited by PubMed Abstract: SNAREs provide the specificity and energy for the fusion of vesicles with their target membrane, but how they are sorted into the appropriate vesicles on post-Golgi trafficking pathways is largely unknown. We demonstrate that the clathrin-mediated endocytosis of the SNARE VAMP7 is directly mediated by Hrb, a clathrin adaptor and ArfGAP. Hrb wraps 20 residues of its unstructured C-terminal tail around the folded VAMP7 longin domain, demonstrating that unstructured regions of clathrin adaptors can select cargo. Disrupting this interaction by mutation of the VAMP7 longin domain or depletion of Hrb causes VAMP7 to accumulate on the cell's surface. However, the SNARE helix of VAMP7 binds back onto its longin domain, outcompeting Hrb for binding to the same groove and suggesting that Hrb-mediated endocytosis of VAMP7 occurs only when VAMP7 is incorporated into a cis-SNARE complex. These results elucidate the mechanism of retrieval of a postfusion SNARE complex in clathrin-coated vesicles. PubMed: 18775314DOI: 10.1016/J.CELL.2008.07.023 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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