Structural genomics plucks high-hanging membrane proteins.

TitleStructural genomics plucks high-hanging membrane proteins.
Publication TypeJournal Article
Year of Publication2012
AuthorsKloppmann, E, Punta, M, Rost, B
JournalCurr Opin Struct Biol
Date Published2012 Jun
KeywordsComputational Biology, Genomics, Humans, Membrane Proteins, Protein Conformation

Recent years have seen the establishment of structural genomics centers that explicitly target integral membrane proteins. Here, we review the advances in targeting these extremely high-hanging fruits of structural biology in high-throughput mode. We observe that the experimental determination of high-resolution structures of integral membrane proteins is increasingly successful both in terms of getting structures and of covering important protein families, for example, from Pfam. Structural genomics has begun to contribute significantly toward this progress. An important component of this contribution is the set up of robotic pipelines that generate a wealth of experimental data for membrane proteins. We argue that prediction methods for the identification of membrane regions and for the comparison of membrane proteins largely suffice to meet the challenges of target selection for structural genomics of membrane proteins. In contrast, we need better methods to prioritize the most promising members in a family of closely related proteins and to annotate protein function from sequence and structure in absence of homology.

Alternate JournalCurr. Opin. Struct. Biol.
PubMed ID22622032
PubMed Central IDPMC3400333
Grant ListU54 GM095315 / GM / NIGMS NIH HHS / United States
U54 GM095315 / GM / NIGMS NIH HHS / United States