1GPL
RP2 LIPASE
1GPL の概要
エントリーDOI | 10.2210/pdb1gpl/pdb |
分子名称 | RP2 LIPASE, CALCIUM ION (3 entities in total) |
機能のキーワード | serine esterase, hydrolase, lipid degradation, pancreas, glycoprotein, chimeric |
由来する生物種 | Cavia porcellus (domestic guinea pig) |
細胞内の位置 | Secreted: P16233 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 47915.92 |
構造登録者 | |
主引用文献 | Withers-Martinez, C.,Carriere, F.,Verger, R.,Bourgeois, D.,Cambillau, C. A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. Structure, 4:1363-1374, 1996 Cited by PubMed Abstract: The guinea pig pancreatic lipase-related protein 2 (GPLRP2) differs from classical pancreatic lipases in that it displays both lipase and phospholipase A1 activities; classical pancreatic lipases have no phospholipase activity. The sequence of GPLRP2 is 63 % identical to that of human pancreatic lipase (HPL), but the so-called lid domain, is much reduced in GPLRP2. A phospholipase A1 from hornet venom (Dolml PLA1) is very similar to HPL and GPLRP2 but is devoid of lipase activity; Dolml PLA1 also contains a reduced lid domain and lacks a region termed the beta9 loop, which is located in the vicinity of the HPL and GPLRP2 active sites. The structure determination of a chimera of GPLRP2 and HPL and domain building of Dolml PLA1 were undertaken to gain a better understanding of the structural parameters responsible for the differences in lipase versus phospholipase activity among these structurally related enzymes. PubMed: 8939760DOI: 10.1016/S0969-2126(96)00143-8 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.01 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
