2JNT
Structure of Bombyx mori Chemosensory Protein 1 in Solution
2JNT の概要
| エントリーDOI | 10.2210/pdb2jnt/pdb |
| NMR情報 | BMRB: 6943 |
| 分子名称 | Chemosensory protein CSP1 (1 entity in total) |
| 機能のキーワード | bmorcsp1, csp1, ligand binding protein |
| 由来する生物種 | Bombyx mori (domestic silkworm) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12558.27 |
| 構造登録者 | Jansen, S.,Zidek, L.,Chmelik, J.,Novak, P.,Padrta, P.,Picimbon, J.,Lofstedt, C.,Sklenar, V. (登録日: 2007-02-02, 公開日: 2007-11-20, 最終更新日: 2024-11-06) |
| 主引用文献 | Jansen, S.,Chmelik, J.,Zidek, L.,Padrta, P.,Novak, P.,Zdrahal, Z.,Picimbon, J.-F.,Lofstedt, C.,Sklenar, V. Structure of Bombyx mori chemosensory protein 1 in solution Arch.Insect Biochem.Physiol., 66:135-145, 2007 Cited by PubMed Abstract: Chemosensory Proteins (CSPs) represent a family of conserved proteins found in insects that may be involved in chemosensory functions. BmorCSP1 is expressed mainly in antennae and legs of the silkworm moth Bombyx mori and was cloned from antennal cDNA. Here we report the determination of the structure of Bombyx mori CSP1 (BmorCSP1) by NMR. The overall fold of BmorCSP1 is globular and comprises six alpha-helices. These helices span residues 10-14, 17-27, 35-49, 57-72, 75-85, and 92-100. The internal hydrophobic sides of the helices are formed mostly by leucine and isoleucine residues and, therefore, well suited to constitute a binding site for hydrophobic ligands. PubMed: 17966128DOI: 10.1002/arch.20205 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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