1VHH
A POTENTIAL CATALYTIC SITE WITHIN THE AMINO-TERMINAL SIGNALLING DOMAIN OF SONIC HEDGEHOG
1VHH の概要
| エントリーDOI | 10.2210/pdb1vhh/pdb |
| 分子名称 | SONIC HEDGEHOG, ZINC ION, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | signalling protein |
| 由来する生物種 | Mus musculus (house mouse) |
| 細胞内の位置 | Sonic hedgehog protein C-product: Secreted, extracellular space. Sonic hedgehog protein N-product: Cell membrane; Lipid-anchor: Q62226 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 18706.34 |
| 構造登録者 | Hall, T.M.T.,Porter, J.A.,Beachy, P.A.,Leahy, D.J. (登録日: 1995-10-03, 公開日: 1996-01-29, 最終更新日: 2024-02-14) |
| 主引用文献 | Hall, T.M.,Porter, J.A.,Beachy, P.A.,Leahy, D.J. A potential catalytic site revealed by the 1.7-A crystal structure of the amino-terminal signalling domain of Sonic hedgehog. Nature, 378:212-216, 1995 Cited by PubMed Abstract: Within the past few years, members of the hedgehog (hh) family of secreted signalling proteins have emerged as the primary signals generated by certain embryonic patterning centres. In vertebrate embryos, for example, sonic hedgehog expression in the notochord appears to be responsible for the local and long-range induction of ventral cell types within the neural tube and somites (reviewed in refs 1, 2). Protein products encoded by hh family members are synthesized as precursors that undergo autoprocessing to generate an amino-terminal domain that appears to be responsible for both local and long-range signalling activities, and a carboxy-terminal domain that contains the autoprocessing activity. As part of an effort to understand how hh family members participate in cell-to-cell signalling, we have determined and report here the crystal structure at 1.7 A of the amino-terminal domain of murine Sonic hedgehog (Shh-N). The structure revealed a tetrahedrally coordinated zinc ion that appears to be structurally analogous to the zinc coordination sites of zinc hydrolases, such as thermolysin and carboxypeptidase A. This previously unsuspected catalytic site represents a distinct activity from the autoprocessing activity that resides in the carboxy-terminal domain. PubMed: 7477329DOI: 10.1038/378212a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






