CREB-binding protein: Difference between revisions

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CBP contains several domains.  Among them the lysine recognition bromodomain; domains KIX, TAZ1 and TAZ2 which bind sequences spanning the transactivation domain of transcription factor p53;  IBiD which binds the interferon response; ZZ is a zinc-binding motif; CH1 (Cys- and His-rich region 1) interacts with the N-terminal of p73.
CBP contains several domains.  Among them the lysine recognition bromodomain; domains KIX, TAZ1 and TAZ2 which bind sequences spanning the transactivation domain of transcription factor p53;  IBiD which binds the interferon response; ZZ is a zinc-binding motif; CH1 (Cys- and His-rich region 1) interacts with the N-terminal of p73.


<scene name='54/541099/Cv/4'>Acetyllysine binding site</scene> with chain A. Water molecules are shown as red spheres.
<scene name='54/541099/Cv/5'>Acetyllysine binding site</scene> with chain A. Water molecules are shown as red spheres.


<scene name='54/541099/Cv/2'>Acetyllysine binding site</scene> with chain B ([[3p1c]]).<ref>PMID:22464331</ref>
<scene name='54/541099/Cv/6'>Acetyllysine binding site</scene> with chain B ([[3p1c]]).<ref>PMID:22464331</ref>
</StructureSection>
</StructureSection>
== 3D Structures of CREB-binding protein ==
== 3D Structures of CREB-binding protein ==

Revision as of 06:56, 18 February 2019

Human CREB-binding protein with acetyllysine complex with SCN- and K+ (purple) ions 3p1c

Drag the structure with the mouse to rotate

3D Structures of CREB-binding protein

Updated on 18-February-2019

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky