2O9O
Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution
「1SV8」から置き換えられました2O9O の概要
| エントリーDOI | 10.2210/pdb2o9o/pdb |
| 関連するPDBエントリー | 2DPE 2ESC |
| 分子名称 | Chitinase-3-like protein 1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| 機能のキーワード | spb-40, tim barrel, signaling protein |
| 由来する生物種 | Bubalus bubalis (water buffalo) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 41853.06 |
| 構造登録者 | Ethayathulla, A.S.,Srivastava, D.B.,Kumar, J.,Sharma, S.,Kaur, P.,Singh, T.P. (登録日: 2006-12-14, 公開日: 2007-01-02, 最終更新日: 2024-10-30) |
| 主引用文献 | Ethayathulla, A.S.,Srivastava, D.B.,Kumar, J.,Saravanan, K.,Bilgrami, S.,Sharma, S.,Kaur, P.,Srinivasan, A.,Singh, T.P. Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution Acta Crystallogr.,Sect.F, 63:258-265, 2007 Cited by PubMed Abstract: The crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 A resolution. SPB-40 acts as a protective signalling factor by binding to viable cells during the early phase of involution, during which extensive tissue remodelling occurs. It was isolated from the dry secretions of Murrah buffalo. It was purified and crystallized using the hanging-drop vapour-diffusion method with 19% ethanol as the precipitant. The protein was also cloned and its complete nucleotide and amino-acid sequences were determined. When compared with the sequences of other members of the family, the sequence of SPB-40 revealed two very important mutations in the sugar-binding region, in which Tyr120 changed to Trp120 and Glu269 changed to Trp269. The structure showed a significant distortion in the shape of the sugar-binding groove. The water structure in the groove is also drastically altered. The folding of the protein chain in the flexible region comprising segments His188-His197, Phe202-Arg212 and Tyr244-Pro260 shows large variations when compared with other proteins of the family. PubMed: 17401190DOI: 10.1107/S1744309107010445 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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