Stereospecific interactions of proline residues in protein structures and complexes

被引:155
作者
Bhattacharyya, R [1 ]
Chakrabarti, P [1 ]
机构
[1] Bose Inst, Dept Biochem, Kolkata 700054, W Bengal, India
关键词
proline; aromatic residues; hydrogen bonding; helix capping; protein-protein interaction;
D O I
10.1016/S0022-2836(03)00759-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The constrained backbone torsion angle of a proline (Pro) residue has usually been invoked to explain its three-dimensional context in proteins. Here we show that specific interactions involving the pyrrolidine ring atoms also contribute to its location in a given secondary structure and its binding to another molecule. It is adept at participating in two rather non-conventional interactions, C-H...pi and C-H...O. The geometry of interaction between the pyrrolidine and aromatic rings, vis-a-vis the occurrence of the C-H...pi interactions has been elucidated. Some of the secondary structural elements stabilized by Pro-aromatic interactions are beta-turns, where a Pro can interact with an adjacent aromatic residue, and in antiparallel beta-sheet, where a Pro in an edge strand can interact with an aromatic residue in the adjacent strand at a non-hydrogen-bonded site. The C-H groups at the C-alpha and C-delta positions can form strong C-H... O interactions (as seen from the clustering of points) and such interactions involving a Pro residue at C' position relative to an alpha-helix can cap the hydrogen bond forming potentials of the free carbonyl groups at the helix C terminus. Functionally important Pro residues occurring at the binding site of a protein almost invariably engage aromatic residues (with one of them being held by C-H...pi interaction) from the partner molecule in the complex, and such aromatic residues are highly conserved during evolution. (C) 2003 Elsevier Ltd. All rights reserved.
引用
收藏
页码:925 / 940
页数:16
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