1y0j

From Proteopedia

(Difference between revisions)

Revision as of 10:28, 6 January 2021

Zinc fingers as protein recognition motifs: structural basis for the GATA-1/Friend of GATA interaction

Structural highlights

1y0j is a 2 chain structure with sequence from Drome and Lk3 transgenic mice. The March 2007 RCSB PDB Molecule of the Month feature on Zinc Fingers by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_3. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1gnf, 1fv5
Gene:	gata-1 (LK3 transgenic mice), u-shaped (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GATA1_MOUSE] Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.^[1] ^[2] ^[3] ^[4] ^[5] [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.^[6] ^[7] ^[8] ^[9] ^[10] ^[11]

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 PubMed

GATA-1 and friend of GATA (FOG) are zinc-finger transcription factors that physically interact to play essential roles in erythroid and megakaryocytic development. Several naturally occurring mutations in the GATA-1 gene that alter the FOG-binding domain have been reported. The mutations are associated with familial anemias and thrombocytopenias of differing severity. To elucidate the molecular basis for the GATA-1/FOG interaction, we have determined the three-dimensional structure of a complex comprising the interaction domains of these proteins. The structure reveals how zinc fingers can act as protein recognition motifs. Details of the architecture of the contact domains and their physical properties provide a molecular explanation for how the GATA-1 mutations contribute to distinct but related genetic diseases.

Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction.,Liew CK, Simpson RJ, Kwan AH, Crofts LA, Loughlin FE, Matthews JM, Crossley M, Mackay JP Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):583-8. Epub 2005 Jan 11. PMID:15644435^[12]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Martin DI, Orkin SH. Transcriptional activation and DNA binding by the erythroid factor GF-1/NF-E1/Eryf 1. Genes Dev. 1990 Nov;4(11):1886-98. PMID:2276623
↑ Crossley M, Orkin SH. Phosphorylation of the erythroid transcription factor GATA-1. J Biol Chem. 1994 Jun 17;269(24):16589-96. PMID:8206977
↑ Calligaris R, Bottardi S, Cogoi S, Apezteguia I, Santoro C. Alternative translation initiation site usage results in two functionally distinct forms of the GATA-1 transcription factor. Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11598-602. PMID:8524811
↑ Collavin L, Gostissa M, Avolio F, Secco P, Ronchi A, Santoro C, Del Sal G. Modification of the erythroid transcription factor GATA-1 by SUMO-1. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8870-5. Epub 2004 Jun 1. PMID:15173587 doi:http://dx.doi.org/10.1073/pnas.0308605101
↑ Lamonica JM, Vakoc CR, Blobel GA. Acetylation of GATA-1 is required for chromatin occupancy. Blood. 2006 Dec 1;108(12):3736-8. Epub 2006 Aug 3. PMID:16888089 doi:http://dx.doi.org/10.1182/blood-2006-07-032847
↑ 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
↑ Liew CK, Simpson RJ, Kwan AH, Crofts LA, Loughlin FE, Matthews JM, Crossley M, Mackay JP. Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):583-8. Epub 2005 Jan 11. PMID:15644435

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y0j"

@@ Line 1: / Line 1: @@
 ==Zinc fingers as protein recognition motifs: structural basis for the GATA-1/Friend of GATA interaction==
-<StructureSection load='1y0j' size='340' side='right' caption='[[1y0j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1y0j' size='340' side='right'caption='[[1y0j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y0j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. The March 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Zinc Fingers''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_3 10.2210/rcsb_pdb/mom_2007_3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y0J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y0j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. The March 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Zinc Fingers''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_3 10.2210/rcsb_pdb/mom_2007_3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y0J FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gnf|1gnf]], [[1fv5|1fv5]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gnf|1gnf]], [[1fv5|1fv5]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gata-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), u-shaped ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0j OCA], [http://pdbe.org/1y0j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y0j RCSB], [http://www.ebi.ac.uk/pdbsum/1y0j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0j ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0j OCA], [http://pdbe.org/1y0j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y0j RCSB], [http://www.ebi.ac.uk/pdbsum/1y0j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0j ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Drome]]
+[[Category: Large Structures]]
 [[Category: Lk3 transgenic mice]]
 [[Category: RCSB PDB Molecule of the Month]]

1y0j

From Proteopedia

Revision as of 10:28, 6 January 2021

Zinc fingers as protein recognition motifs: structural basis for the GATA-1/Friend of GATA interaction

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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