1uzc: Difference between revisions
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uzc ConSurf]. | ||
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Revision as of 06:06, 10 February 2016
THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold. The structure of an FF domain from human HYPA/FBP11.,Allen M, Friedler A, Schon O, Bycroft M J Mol Biol. 2002 Oct 25;323(3):411-6. PMID:12381297[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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