Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1PCN

SOLUTION STRUCTURE OF PORCINE PANCREATIC PROCOLIPASE AS DETERMINED FROM 1H HOMONUCLEAR TWO-AND THREE-DIMENSIONAL NMR

1PCN の概要
エントリーDOI10.2210/pdb1pcn/pdb
分子名称PORCINE PANCREATIC PROCOLIPASE B (1 entity in total)
機能のキーワードlipase protein cofactor
由来する生物種Sus scrofa (pig)
タンパク質・核酸の鎖数1
化学式量合計10117.49
構造登録者
Breg, J.N.,Sarda, L.,Cozzone, P.J.,Rugani, N.,Boelens, R.,Kaptein, R. (登録日: 1994-06-08, 公開日: 1994-12-20, 最終更新日: 2024-11-06)
主引用文献Breg, J.N.,Sarda, L.,Cozzone, P.J.,Rugani, N.,Boelens, R.,Kaptein, R.
Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR.
Eur.J.Biochem., 227:663-672, 1995
Cited by
PubMed Abstract: Procolipase is the precursor of colipase, which acts as protein cofactor for the activity of pancreatic lipase. The solution structure of procolipase has been determined by 1H NMR using two- and three-dimensional measurements. The secondary structure determination identified two separate three-stranded beta-sheet regions with concomitant hydrogen bond patterns. The tertiary structure of the protein was determined using 863 non-trivial proton--proton distance constraints, 14 hydrogen bond distance constraints and 55 phi and 25 X1 dihedral constraints. The structure that was obtained from distance geometry and energy refinement contains three highly disordered loops as well as a disordered N- and C-terminal region. The remaining part of the structure is well defined with a root-mean-square deviation (rmsd) relative to the average of 0.09 +/- 0.02 nm for backbone atoms (residues 11-30, 37-50, 57-69, 83-89). The protein comprises two identical domains, each containing a three-strand beta-sheet and two disulfide bonds: a 15-residue region in each domain superimposes with 0.07 nm rmsd, measured on backbone atoms. The solution structure is nearly identical to the crystal structure. It is in agreement with previous NMR data and, in combination with these data, supports the current model of procolipase micelle interaction and the lipase activation by colipase.
PubMed: 7867624
DOI: 10.1111/j.1432-1033.1995.tb20186.x
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1pcn
検証レポート(詳細版)ダウンロードをダウンロード

248636

件を2026-02-04に公開中

PDB statisticsPDBj update infoContact PDBjnumon