1fv5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (18:36, 29 November 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1fv5.png|left|200px]]
 
-
<!--
+
==SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR==
-
The line below this paragraph, containing "STRUCTURE_1fv5", creates the "Structure Box" on the page.
+
<StructureSection load='1fv5' size='340' side='right'caption='[[1fv5]]' 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'>[[1fv5]] 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=1FV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FV5 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_1fv5| PDB=1fv5 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fv5 OCA], [https://pdbe.org/1fv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fv5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fv5 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 ==
 +
BACKGROUND: Zinc finger domains have traditionally been regarded as sequence-specific DNA binding motifs. However, recent evidence indicates that many zinc fingers mediate specific protein-protein interactions. For instance, several zinc fingers from FOG family proteins have been shown to interact with the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to determine the first structures of two FOG family zinc fingers that are involved in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers resemble classical TFIIIA-like zinc fingers, with the exception of an unusual extended portion of the polypeptide backbone prior to the fourth zinc ligand. [15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of USH-F1, and comparison with other FOG family proteins indicates that the recognition mechanism is conserved across species. The surface of FOG-type fingers that interacts with GATA-1 overlaps substantially with the surface through which classical fingers typically recognize DNA. This suggests that these fingers could not contact both GATA and DNA simultaneously. In addition, results from NMR, gel filtration, and sedimentation equilibrium experiments suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results demonstrate unequivocally that zinc fingers comprising the classical betabetaalpha fold are capable of mediating specific contacts between proteins. The existence of this alternative function has implications for the prediction of protein function from sequence data and for the evolution of protein function.
-
===SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR===
+
Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions.,Liew CK, Kowalski K, Fox AH, Newton A, Sharpe BK, Crossley M, Mackay JP Structure. 2000 Nov 15;8(11):1157-66. PMID:11080638<ref>PMID:11080638</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_11080638}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1fv5" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 11080638 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_11080638}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1FV5 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=1FV5 OCA].
+
-
 
+
-
==Reference==
+
-
Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions., Liew CK, Kowalski K, Fox AH, Newton A, Sharpe BK, Crossley M, Mackay JP, Structure. 2000 Nov 15;8(11):1157-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080638 11080638]
+
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Crossley, M.]]
+
[[Category: Crossley M]]
-
[[Category: Fox, A H.]]
+
[[Category: Fox AH]]
-
[[Category: Kowalski, K.]]
+
[[Category: Kowalski K]]
-
[[Category: Liew, C K.]]
+
[[Category: Liew CK]]
-
[[Category: Mackay, J P.]]
+
[[Category: Mackay JP]]
-
[[Category: Newton, A.]]
+
[[Category: Newton A]]
-
[[Category: Sharpe, B K.]]
+
[[Category: Sharpe BK]]
-
[[Category: Cchc]]
+
-
[[Category: Protein interaction]]
+
-
[[Category: Zinc finger]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:59:32 2008''
+

Current revision

SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR

PDB ID 1fv5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fv5"
Personal tools