1jn7: Difference between revisions
New page: left|200px<br /><applet load="1jn7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jn7" /> '''Solution Structure of a CCHH mutant of the n... |
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[[Image:1jn7.jpg|left|200px]]<br /><applet load="1jn7" size=" | [[Image:1jn7.jpg|left|200px]]<br /><applet load="1jn7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Solution Structure of a CCHH mutant of the ninth CCHC Zinc Finger of U-shaped'''<br /> | '''Solution Structure of a CCHH mutant of the ninth CCHC Zinc Finger of U-shaped'''<br /> | ||
==Overview== | ==Overview== | ||
The N-terminal zinc finger (ZnF) from GATA transcription factors mediates | The N-terminal zinc finger (ZnF) from GATA transcription factors mediates interactions with FOG family proteins. In FOG proteins, the interacting domains are also ZnFs; these domains are related to classical CCHH fingers but have an His --> Cys substitution at the final zinc-ligating position. Here we demonstrate that different CCHC fingers in the FOG family protein U-shaped contact the N-terminal ZnF of GATA-1 in the same fashion although with different affinities. We also show that these interactions are of moderate affinity, which is interesting given the presumed low concentrations of these proteins in the nucleus. Furthermore, we demonstrate that the variant CCHC topology enhances binding affinity, although the His --> Cys change is not essential for the formation of a stably folded domain. To ascertain the structural basis for the contribution of the CCHC arrangement, we have determined the structure of a CCHH mutant of finger nine from U-shaped. The structure is very similar overall to the wild-type domain, with subtle differences at the C terminus that result in loss of the interaction in vivo. Taken together, these results suggest that the CCHC zinc binding topology is required for the integrity of GATA-FOG interactions and that weak interactions can play important roles in vivo. | ||
==About this Structure== | ==About this Structure== | ||
1JN7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1JN7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JN7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kowalski, K.]] | [[Category: Kowalski, K.]] | ||
[[Category: Mackay, J | [[Category: Mackay, J P.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: protein-protein interaction]] | [[Category: protein-protein interaction]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:33 2008'' | ||
Revision as of 14:24, 21 February 2008
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Solution Structure of a CCHH mutant of the ninth CCHC Zinc Finger of U-shaped
OverviewOverview
The N-terminal zinc finger (ZnF) from GATA transcription factors mediates interactions with FOG family proteins. In FOG proteins, the interacting domains are also ZnFs; these domains are related to classical CCHH fingers but have an His --> Cys substitution at the final zinc-ligating position. Here we demonstrate that different CCHC fingers in the FOG family protein U-shaped contact the N-terminal ZnF of GATA-1 in the same fashion although with different affinities. We also show that these interactions are of moderate affinity, which is interesting given the presumed low concentrations of these proteins in the nucleus. Furthermore, we demonstrate that the variant CCHC topology enhances binding affinity, although the His --> Cys change is not essential for the formation of a stably folded domain. To ascertain the structural basis for the contribution of the CCHC arrangement, we have determined the structure of a CCHH mutant of finger nine from U-shaped. The structure is very similar overall to the wild-type domain, with subtle differences at the C terminus that result in loss of the interaction in vivo. Taken together, these results suggest that the CCHC zinc binding topology is required for the integrity of GATA-FOG interactions and that weak interactions can play important roles in vivo.
About this StructureAbout this Structure
1JN7 is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Characterization of the conserved interaction between GATA and FOG family proteins., Kowalski K, Liew CK, Matthews JM, Gell DA, Crossley M, Mackay JP, J Biol Chem. 2002 Sep 20;277(38):35720-9. Epub 2002 Jul 10. PMID:12110675
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