TY - JOUR
T1 - Progress in structure prediction of α-helical membrane proteins
AU - Fleishman, Sarel J.
AU - Ben-Tal, Nir
N1 - Funding Information:
The authors thank SE Harrington, JU Bowie, J Skolnick, O Kalid and CG Tate for critical reading, and B Honig, LR Forrest, L Adamian, J Liang, CG Tate and DT Jones for providing manuscripts before publication. This study was supported by a grant 222/04 from the Israel Science Foundation to N B-T. SJF was supported by a doctoral fellowship from the Clore Israel Foundation.
PY - 2006/8
Y1 - 2006/8
N2 - Transmembrane (TM) proteins comprise 20-30% of the genome but, because of experimental difficulties, they represent less than 1% of the Protein Data Bank. The dearth of membrane protein structures makes computational prediction a potentially important means of obtaining novel structures. Recent advances in computational methods have been combined with experimental data to constrain the modeling of three-dimensional structures. Furthermore, threading and ab initio modeling approaches that were effective for soluble proteins have been applied to TM domains. Surprisingly, experimental structures, proteomic analyses and bioinformatics have revealed unexpected architectures that counter long-held views on TM protein structure and stability. Future computational and experimental studies aimed at understanding the thermodynamic and evolutionary bases of these architectural details will greatly enhance predictive capabilities.
AB - Transmembrane (TM) proteins comprise 20-30% of the genome but, because of experimental difficulties, they represent less than 1% of the Protein Data Bank. The dearth of membrane protein structures makes computational prediction a potentially important means of obtaining novel structures. Recent advances in computational methods have been combined with experimental data to constrain the modeling of three-dimensional structures. Furthermore, threading and ab initio modeling approaches that were effective for soluble proteins have been applied to TM domains. Surprisingly, experimental structures, proteomic analyses and bioinformatics have revealed unexpected architectures that counter long-held views on TM protein structure and stability. Future computational and experimental studies aimed at understanding the thermodynamic and evolutionary bases of these architectural details will greatly enhance predictive capabilities.
UR - http://www.scopus.com/inward/record.url?scp=33746586953&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2006.06.003
DO - 10.1016/j.sbi.2006.06.003
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AN - SCOPUS:33746586953
SN - 0959-440X
VL - 16
SP - 496
EP - 504
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 4
ER -