Advances in comparative protein-structure modelling

Roberto Sánchez, Andrej Šali

Research output: Contribution to journalArticlepeer-review

271 Scopus citations

Abstract

Comparative modelling of protein 3D structure can now be applied with reasonable accuracy to ten times more protein sequences than the number of experimentally determined protein structures. A protein sequence that has at least 40% identity to a known structure can be modelled automatically with an accuracy approaching that of a low resolution X-ray structure or a medium resolution NMR structure. Currently, the errors in comparative models include mistakes in the packing of sidechains, in the conformation and shifts of the core segments and loops, and, most importantly, in an incorrect alignment of the modelled sequence with related known structures. Nevertheless, the number of applications in which comparative modelling has been proven to be useful has grown rapidly.

Original languageEnglish
Pages (from-to)206-214
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume7
Issue number2
DOIs
StatePublished - Apr 1997
Externally publishedYes

Fingerprint

Dive into the research topics of 'Advances in comparative protein-structure modelling'. Together they form a unique fingerprint.

Cite this