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- | {{Seed}} | |
- | [[Image:1jn7.png|left|200px]] | |
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- | <!-- | + | ==Solution Structure of a CCHH mutant of the ninth CCHC Zinc Finger of U-shaped== |
- | The line below this paragraph, containing "STRUCTURE_1jn7", creates the "Structure Box" on the page.
| + | <StructureSection load='1jn7' size='340' side='right'caption='[[1jn7]]' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1jn7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JN7 FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | {{STRUCTURE_1jn7| PDB=1jn7 | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jn7 OCA], [https://pdbe.org/1jn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jn7 RCSB], [https://www.ebi.ac.uk/pdbsum/1jn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jn7 ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/USH_DROME USH_DROME] Transcription regulator that modulates expression mediated by transcription factors of the GATA family such as pnr and srp. Represses transcription of proneural achaete-scute complex (AS-C), which is usually activated by pnr. Involved in cardiogenesis, blood, and eye development. During hematopoiesis, it is required to restrict the number of crystal cells, probably via its interaction with the isoform SrpNC of srp. Negatively regulates expression of sr. Probably acts by interacting with the GATA-type zinc finger of proteins such as pnr and srp, possibly antagonizing the interaction between the GATA-type zinc finger and some cofactor.<ref>PMID:9367989</ref> <ref>PMID:9367990</ref> <ref>PMID:10861002</ref> <ref>PMID:11404479</ref> <ref>PMID:12374748</ref> <ref>PMID:12782269</ref> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | 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. |
| | | |
- | ===Solution Structure of a CCHH mutant of the ninth CCHC Zinc Finger of U-shaped===
| + | 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<ref>PMID:12110675</ref> |
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- | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | <!--
| + | </div> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_12110675}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 1jn7" style="background-color:#fffaf0;"></div> |
- | (as it appears on PubMed at http://www.pubmed.gov), where 12110675 is the PubMed ID number.
| + | == References == |
- | -->
| + | <references/> |
- | {{ABSTRACT_PUBMED_12110675}}
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure== | + | |
- | 1JN7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JN7 OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12110675 12110675]
| + | |
| [[Category: Drosophila melanogaster]] | | [[Category: Drosophila melanogaster]] |
- | [[Category: Single protein]] | + | [[Category: Large Structures]] |
- | [[Category: Kowalski, K.]] | + | [[Category: Kowalski K]] |
- | [[Category: Mackay, J P.]] | + | [[Category: Mackay JP]] |
- | [[Category: Protein-protein interaction]]
| + | |
- | [[Category: Transcription]]
| + | |
- | [[Category: Zinc finger]]
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- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:30:07 2008''
| + | |
| Structural highlights
Function
USH_DROME Transcription regulator that modulates expression mediated by transcription factors of the GATA family such as pnr and srp. Represses transcription of proneural achaete-scute complex (AS-C), which is usually activated by pnr. Involved in cardiogenesis, blood, and eye development. During hematopoiesis, it is required to restrict the number of crystal cells, probably via its interaction with the isoform SrpNC of srp. Negatively regulates expression of sr. Probably acts by interacting with the GATA-type zinc finger of proteins such as pnr and srp, possibly antagonizing the interaction between the GATA-type zinc finger and some cofactor.[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
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.
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[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cubadda Y, Heitzler P, Ray RP, Bourouis M, Ramain P, Gelbart W, Simpson P, Haenlin M. u-shaped encodes a zinc finger protein that regulates the proneural genes achaete and scute during the formation of bristles in Drosophila. Genes Dev. 1997 Nov 15;11(22):3083-95. PMID:9367989
- ↑ Haenlin M, Cubadda Y, Blondeau F, Heitzler P, Lutz Y, Simpson P, Ramain P. Transcriptional activity of pannier is regulated negatively by heterodimerization of the GATA DNA-binding domain with a cofactor encoded by the u-shaped gene of Drosophila. Genes Dev. 1997 Nov 15;11(22):3096-108. PMID:9367990
- ↑ Fossett N, Zhang Q, Gajewski K, Choi CY, Kim Y, Schulz RA. The multitype zinc-finger protein U-shaped functions in heart cell specification in the Drosophila embryo. Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7348-53. PMID:10861002
- ↑ Fossett N, Tevosian SG, Gajewski K, Zhang Q, Orkin SH, Schulz RA. The Friend of GATA proteins U-shaped, FOG-1, and FOG-2 function as negative regulators of blood, heart, and eye development in Drosophila. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7342-7. Epub 2001 Jun 12. PMID:11404479 doi:http://dx.doi.org/10.1073/pnas.131215798
- ↑ Waltzer L, Bataille L, Peyrefitte S, Haenlin M. Two isoforms of Serpent containing either one or two GATA zinc fingers have different roles in Drosophila haematopoiesis. EMBO J. 2002 Oct 15;21(20):5477-86. PMID:12374748
- ↑ Ghazi A, Paul L, VijayRaghavan K. Prepattern genes and signaling molecules regulate stripe expression to specify Drosophila flight muscle attachment sites. Mech Dev. 2003 May;120(5):519-28. PMID:12782269
- ↑ Kowalski K, Liew CK, Matthews JM, Gell DA, Crossley M, Mackay JP. Characterization of the conserved interaction between GATA and FOG family proteins. J Biol Chem. 2002 Sep 20;277(38):35720-9. Epub 2002 Jul 10. PMID:12110675 doi:http://dx.doi.org/10.1074/jbc.M204663200
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