Polyproline-II helix in proteins: structure and function.
作者： Alexei A. Adzhubei , Michael J.E. Sternberg , Alexander A. Makarov
DOI: 10.1016/J.JMB.2013.03.018
关键词: Polyproline helix 、 Biochemistry 、 Protein Data Bank (RCSB PDB) 、 Helix 、 Protein–protein interaction 、 Protein secondary structure 、 Protein structure 、 Protein complex assembly 、 Binding site 、 Biology
摘要: … and β-structure, the left-handed, extended PPII helix represents the … unfolded proteins have a high content of the PPII helices … a relatively strong presence of helical conformations, which …
elsevier.com
sci-hub.se 参考文章(220)
C. Freund, H. -G. Schmalz, J. Sticht, R. Kühne, Proline-Rich Sequence Recognition Domains (PRD) : Ligands, Function and Inhibition Handbook of experimental pharmacology. ,vol. 186, pp. 407- 429 ,(2008) , 10.1007/978-3-540-72843-6_17
Andrea Musacchio, How SH3 domains recognize proline Advances in Protein Chemistry. ,vol. 61, pp. 211- 268 ,(2002) , 10.1016/S0065-3233(02)61006-X
B. M. Jockusch, K. Murk, M. Rothkegel, The profile of profilins Reviews of Physiology Biochemistry and Pharmacology. ,vol. 159, pp. 131- 149 ,(2007) , 10.1007/112_2007_704
Walter Pirovano, Jaap Heringa, Protein secondary structure prediction. Methods of Molecular Biology. ,vol. 609, pp. 327- 348 ,(2010) , 10.1007/978-1-60327-241-4_19
Margaret N. Campbell, Trevor P. Creamer, Determinants of the polyproline II helix from modeling studies Unfolded Proteins. ,vol. 62, pp. 263- 282 ,(2002) , 10.1016/S0065-3233(02)62010-8
W. Austin Elam, Travis P. Schrank, Vincent J. Hilser, Experimental and Computational Studies of Polyproline II Propensity John Wiley & Sons, Inc.. pp. 159- 185 ,(2012) , 10.1002/9781118183373.CH6
Zhengshuang Shi, Robert W. Woody, Neville R. Kallenbach, Is polyproline II a major backbone conformation in unfolded proteins? Unfolded Proteins. ,vol. 62, pp. 163- 240 ,(2002) , 10.1016/S0065-3233(02)62008-X
Bettina Bommarius, David Maxwell, Alyson Swimm, Sara Leung, Anita Corbett, William Bornmann, Daniel Kalman, Enteropathogenic Escherichia coli Tir is an SH2/3 ligand that recruits and activates tyrosine kinases required for pedestal formation Molecular Microbiology. ,vol. 63, pp. 1748- 1768 ,(2007) , 10.1111/J.1365-2958.2007.05626.X
Francis C Peterson, Brian F Volkman, Diversity of polyproline recognition by EVH1 domains Frontiers in Bioscience. ,vol. Volume, pp. 833- 846 ,(2009) , 10.2741/3281
N. Sreerama, Structural composition of betaI- and betaII-proteins Protein Science. ,vol. 12, pp. 384- 388 ,(2003) , 10.1110/PS.0235003