2bfq: Difference between revisions
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==MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES== | ==MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES== | ||
<StructureSection load='2bfq' size='340' side='right' caption='[[2bfq]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2bfq' size='340' side='right'caption='[[2bfq]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bfq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2bfq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFQ FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Arcfl]] | [[Category: Arcfl]] | ||
[[Category: Large Structures]] | |||
[[Category: Allen, M D]] | [[Category: Allen, M D]] | ||
[[Category: Buhecha, H R]] | [[Category: Buhecha, H R]] | ||
Revision as of 22:23, 11 December 2019
MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULESMACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES
Structural highlights
Function[Y1521_ARCFU] Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1-phosphate (Appr1p), but with low efficiency.[1] [2] 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 ADP-ribosylation of proteins is an important post-translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose. The macro domain is an ADP-ribose binding module.,Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:15902274[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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