1REI

THE MOLECULAR STRUCTURE OF A DIMER COMPOSED OF THE VARIABLE PORTIONS OF THE BENCE-JONES PROTEIN REI REFINED AT 2.0 ANGSTROMS RESOLUTION

1REI の概要

• エントリーDOI: 10.2210/pdb1rei/pdb
• 分子名称: BENCE-JONES PROTEIN REI (LIGHT CHAIN) (2 entities in total)
• 機能のキーワード: immunoglobulin(part)sequesters antigens
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23503.98

構造登録者

Epp, O.,Lattman, E.E.,Colman, P.,Fehlhammer, H.,Bode, W.,Schiffer, M.,Huber, R.,Palm, W. (登録日: 1976-03-17, 公開日: 1976-05-19, 最終更新日: 2024-10-23)

主引用文献

Epp, O.,Lattman, E.E.,Schiffer, M.,Huber, R.,Palm, W.
The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-A resolution.
Biochemistry, 14:4943-4952, 1975

PubMed Abstract: The structure of the variable portions of a K-type Bence-Jones protein REI forming a dimer has been determined by X-ray diffraction to a resolution of 2.0 A. The structure has been refined using a constrained crystallographic refinement procedure. The final R value is 0.24 for 15000 significantly measured reflections; the estimated standard deviation of atomic positions is 0.09 A. A more objective assessment of the error in the atomic positions is possible by comparing the two independently refined monomers. The mean deviation of main-chain atoms of the two chains in internal segments in 0.22 A, of main-chain dihedral angles 6.3 degrees for these segments. The unrefined molecular structure of the VREI dimer has been published (Epp, O., Colman, P., Fehlhammer, H., Bode, W., Schiffer, M., Huber, R., and Palm, W. (1974), Eur. J. Biochem. 45, 513). Now a detailed analysis is presented in terms of hydrogen bonds and conformational angles. Secondary structural elements (antiparallel beta structure, reverse turns) are defined. A more precise atomic arrangement of the amino acid residues forming the contact region and the hapten binding site is given as well as the localization of solvent molecules. Two cis-prolines (Pro-8 and Pro-95) were detected. The intrachain disulfide bridge (Cys-23-Cys-88) occurs statistically in two alternative conformations. The structure suggests reasons for strong conservation of several amino acid residues. The knowledge of the refined molecular structure enables crystal structure analyses of related molecules to be made by Patterson search techniques. The calculated phases based on the refined structure are much improved compared to isomorphous phases. Therefore the effects of hapten binding on the molecular structure can be analyzed by the difference Fourier technique with more reliability. Hapten binding studies have been started.

PubMed: 1182131
DOI: 10.1021/bi00693a025

実験手法

X-RAY DIFFRACTION (2 Å)