1BM5

THE SOLUTION STRUCTURE OF A SITE-DIRECTED MUTANT (R111M) OF HUMAN CELLULAR RETIONIC ACID BINDING PROTEIN-TYPE II, NMR, 31 STRUCTURES

1BM5 の概要

• エントリーDOI: 10.2210/pdb1bm5/pdb
• 分子名称: CELLULAR RETINOIC ACID BINDING PROTEIN-TYPE II (1 entity in total)
• 機能のキーワード: retinoic-acid transport, crabpii
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15555.80

構造登録者

Wang, H.,Yan, H. (登録日: 1998-07-28, 公開日: 1999-01-13, 最終更新日: 2024-05-22)

主引用文献

Wang, L.,Yan, H.
NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Biochemistry, 37:13021-13032, 1998

PubMed Abstract: The solution structure of a site-directed mutant of type-II human cellular retinoic acid binding protein (CRABPII) with Arg111 replaced by methionine (R111M) has been determined by NMR spectroscopy. The sequential assignments of the 1H and 15N resonances of apo-R111M were established by multinuclear multidimensional NMR. The solution structure was calculated from 2302 distance restraints and 77 phi dihedral restraints derived from the NMR data. The root-mean-square deviation of the ensemble of 28 refined conformers that represent the structure from the mean coordinate set derived from them was 0.54 +/- 0.26 and 0.98 +/- 0.23 A for the backbone atoms and all heavy atoms, respectively. The solution structure of apo-R111M is similar to that of wild-type apo-CRABPII. However, there are significant conformational differences between the two proteins, localized mainly to three segments (Leu19-Ala36, Glu73-Cys81, and Leu99-Pro105) clustered around the ligand entrance more than 17 A away from the point mutation. In apo-R111M, all the three segments move toward the center of the ligand entrance so that the opening of the ligand-binding pocket in apo-R111M is much smaller than that in wild-type apo-CRABPII. Furthermore, the ligand-binding pocket of apo-R111M, especially the ligand entrance, is much less flexible than that of apo-CRABPII. Surprisingly, apo-R111M is more similar to holo-CRABPII than to apo-CRABPII in both structure and dynamical properties. The conformational and dynamical changes caused by the mutation are similar to those induced by binding of RA, although the magnitudes of the changes caused by the mutation are smaller than those induced by binding of RA. The results suggest that Arg111 plays a critical role in determining the structure and dynamical properties of CRABPII.

PubMed: 9737883
DOI: 10.1021/bi981021x

実験手法

SOLUTION NMR