1CCD

REFINED STRUCTURE OF RAT CLARA CELL 17 KDA PROTEIN AT 3.0 ANGSTROMS RESOLUTION

1CCD の概要

• エントリーDOI: 10.2210/pdb1ccd/pdb
• 分子名称: CLARA CELL 17 kD PROTEIN, SULFATE ION (2 entities in total)
• 機能のキーワード: phospholipase a2 inhibitor
• 由来する生物種: Rattus rattus (black rat)
• 細胞内の位置: Secreted: P17559
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8571.74

構造登録者

Umland, T.C.,Swaminathan, S.,Furey, W.,Singh, G.,Pletcher, J.,Sax, M. (登録日: 1991-09-17, 公開日: 1994-01-31, 最終更新日: 2024-10-09)

主引用文献

Umland, T.C.,Swaminathan, S.,Furey, W.,Singh, G.,Pletcher, J.,Sax, M.
Refined structure of rat Clara cell 17 kDa protein at 3.0 A resolution.
J.Mol.Biol., 224:441-448, 1992

PubMed Abstract: The rat Clara cell 17 kDa protein (previously referred to as the rat Clara cell 10 kDa protein) has been reported to inhibit phospholipase A2 and papain, and to also bind progesterone. It has been isolated from rat lung lavage fluid and crystallized in the space group P6(5)22. The structure has been determined to 3.0 A resolution using the molecular replacement method. Uteroglobin, whose amino acid sequence is 55.7% identical, was used as the search model. The structure was then refined using restrained least-squares and simulated annealing methods. The R-factor is 22.5%. The protein is a covalently bound dimer. Two disulfide bonds join the monomers together in an antiparallel manner such that the dimer encloses a large internal hydrophobic cavity. The hydrophobic cavity is large enough to serve as the progesterone binding site, but access to the cavity is limited. Each monomer is composed of four alpha-helices. The main-chain structure of the Clara cell protein closely resembles that of uteroglobin, but the nature of many of the exposed side-chains differ. This is true, particularly in a hypervariable region between residues 23 and 36, and in the H1H4 pocket.

PubMed: 1560460
DOI: 10.1016/0022-2836(92)91006-B

実験手法

X-RAY DIFFRACTION (3 Å)