1BBA

SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SOLUTION STRUCTURE OF BOVINE PANCREATIC POLYPEPTIDE

1BBA の概要

• エントリーDOI: 10.2210/pdb1bba/pdb
• 分子名称: BOVINE PANCREATIC POLYPEPTIDE (1 entity in total)
• 機能のキーワード: pancreatic hormone
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4230.74

構造登録者

Li, X.,Sutcliffe, M.J.,Schwartz, T.W.,Dobson, C.M. (登録日: 1992-03-10, 公開日: 1993-10-31, 最終更新日: 2024-05-22)

主引用文献

Li, X.A.,Sutcliffe, M.J.,Schwartz, T.W.,Dobson, C.M.
Sequence-specific 1H NMR assignments and solution structure of bovine pancreatic polypeptide.
Biochemistry, 31:1245-1253, 1992

PubMed Abstract: Sequence-specific 1H NMR assignments for the 36 residue bovine pancreatic polypeptide (bPP) have been completed. The secondary and tertiary structure of bPP in solution has been determined from experimental NMR data. It is shown that bPP has a very well-defined C-terminal alpha-helix involving residues 15-32. Although regular secondary structure cannot be clearly defined in the N-terminal region, residues 4-8 maintain a rather ordered conformation in solution. This is attributed primarily to the hydrophobic interactions between this region and the C-terminal helix. The two segments of the structure are joined by a turn which is poorly defined. The four end residues both at the N-terminus and the C-terminus are highly disordered in solution. The overall fold of the bPP molecule is very closely similar to that found in the crystal structure of avian pancreatic polypeptide (aPP). The RMS deviation for backbone atoms of residues 4-8 and 15-32 between the bPP mean structure and the aPP crystal structure is 0.65 A, although there is only 39% identity of the residues. Furthermore, the average conformations of some (mostly from the alpha-helix) side chains of bPP in solution are closely similar to those of aPP in the crystal structure. A large number of side chains of bPP, however, show significant conformational averaging in solution.

PubMed: 1734969
DOI: 10.1021/bi00119a038

実験手法

SOLUTION NMR