Directional shape complementarity at the protein-DNA interface.

@article{citeulike:620736, abstract = {Nature utilizes various styles of architecture for DNA-binding proteins to recognize diverse DNA sequences, a process facilitated by a complementary surface between protein and DNA. However, the extent and ways this 'shape complementarity' occurs at the protein-DNA interface have yet to be characterized. Here, by analyzing a set of diverse protein-DNA complexes of known three-dimensional structures, we investigated whether the normal vectors of a protein surface at the interface exhibited any relationship with DNA conformation. Generally, the normal vectors of a DNA-contacting protein surface distinctly preferred certain angles, enabling them to align with certain axes characterizing the conformation of DNA. Thus, a new geometric property of DNA-binding protein is demonstrated, i.e. the "shape complementarity" of protein-DNA recognition clearly bears the property of "directionality".}, address = {MedicoGenomic Research Center, Kaohsiung Medical University, 100 Shih-Chuan 1st Road, Kaohsiung 807, Taiwan, Republic of China.}, author = {Yeh, C. S. and Chen, F. M. and Wang, J. Y. and Cheng, T. L. and Hwang, M. J. and Tzou, W. S. }, citeulike-article-id = {620736}, doi = {10.1002/jmr.624}, issn = {0952-3499}, journal = {J Mol Recognit}, keywords = {protein-dna\_interaction}, number = {4}, pages = {213--222}, posted-at = {2007-06-14 16:10:20}, priority = {2}, title = {Directional shape complementarity at the protein-DNA interface.}, url = {http://dx.doi.org/10.1002/jmr.624}, volume = {16}, year = {2003} }

TY - JOUR ID - citeulike:620736 L3 - citeulike-article-id:620736 TI - Directional shape complementarity at the protein-DNA interface. JF - J Mol Recognit VL - 16 IS - 4 SP - 213 EP - 222 AD - MedicoGenomic Research Center, Kaohsiung Medical University, 100 Shih-Chuan 1st Road, Kaohsiung 807, Taiwan, Republic of China. SN - 0952-3499 N2 - Nature utilizes various styles of architecture for DNA-binding proteins to recognize diverse DNA sequences, a process facilitated by a complementary surface between protein and DNA. However, the extent and ways this 'shape complementarity' occurs at the protein-DNA interface have yet to be characterized. Here, by analyzing a set of diverse protein-DNA complexes of known three-dimensional structures, we investigated whether the normal vectors of a protein surface at the interface exhibited any relationship with DNA conformation. Generally, the normal vectors of a DNA-contacting protein surface distinctly preferred certain angles, enabling them to align with certain axes characterizing the conformation of DNA. Thus, a new geometric property of DNA-binding protein is demonstrated, i.e. the "shape complementarity" of protein-DNA recognition clearly bears the property of "directionality". KW - protein-dna_interaction AU - Yeh, CS AU - Chen, FM AU - Wang, JY AU - Cheng, TL AU - Hwang, MJ AU - Tzou, WS PY - 2003///g UR - http://dx.doi.org/10.1002/jmr.624 ER -