1uzc: Difference between revisions
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==THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11== | ==THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11== | ||
<StructureSection load='1uzc' size='340' side='right' caption='[[1uzc]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''> | <StructureSection load='1uzc' size='340' side='right'caption='[[1uzc]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1uzc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1h40 1h40]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UZC FirstGlance]. <br> | <table><tr><td colspan='2'>[[1uzc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1h40 1h40]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UZC FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Allen, M D]] | [[Category: Allen, M D]] | ||
[[Category: Bycroft, M]] | [[Category: Bycroft, M]] | ||
Revision as of 14:27, 4 December 2019
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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