1PTS

CRYSTAL STRUCTURE AND LIGAND BINDING STUDIES OF A SCREENED PEPTIDE COMPLEXED WITH STREPTAVIDIN

1PTS の概要

• エントリーDOI: 10.2210/pdb1pts/pdb
• 分子名称: STREPTAVIDIN, PEPTIDE (FSHPQNT) (3 entities in total)
• 機能のキーワード: glycoprotein, biotin-binding protein-peptide complex, biotin-binding protein/peptide
• 由来する生物種: Streptomyces avidinii
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 26308.32

構造登録者

Weber, P.C.,Pantoliano, M.W.,Thompson, L.D. (登録日: 1992-07-23, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Weber, P.C.,Pantoliano, M.W.,Thompson, L.D.
Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin.
Biochemistry, 31:9350-9354, 1992

PubMed Abstract: The thermodynamic binding parameters and crystal structure for streptavidin-peptide complexes where the peptide sequences were obtained by random screening methods are reported. The affinities between streptavidin and two heptapeptides were determined by titrating calorimetric methods [Phe-Ser-His-Pro-Gln-Asn-Thr, Ka = 7944 (+/- 224) M-1, delta G degrees = -5.32 (+/- 0.01) kcal/mol, and delta H degrees = -19.34 (+/- 0.48) kcal/mol; His-Asp-His-Pro-Gln-Asn-Leu, Ka = 3542 (+/- 146) M-1, delta G degrees = -4.84 (+/- 0.03) kcal/mol, and delta H degrees = -19.00 (+/- 0.64) kcal/mol]. The crystal structure of streptavidin complexed with one of these peptides has been determined at 2.0-A resolution. The peptide (Phe-Ser-His-Pro-Gln-Asn-Thr) binds in a turn conformation with the histidine, proline, and glutamine side chains oriented inward at the biotin-binding site. A water molecule is immobilized between the histidine and glutamine side chains of the peptide and an aspartic acid side chain of the protein. Although some of the residues that participate in binding biotin also interact with the screened peptide, the peptide adopts an alternate method of utilizing binding determinants in the biotin-binding site of streptavidin.

PubMed: 1390720
DOI: 10.1021/bi00154a004

実験手法

X-RAY DIFFRACTION (2 Å)