6ako

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:36, 22 November 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6ako is ON HOLD
+
==Crystal Structure of FOXC2 DBD Bound to DBE2 DNA==
 +
<StructureSection load='6ako' size='340' side='right'caption='[[6ako]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6ako]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AKO FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.396&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ako FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ako OCA], [https://pdbe.org/6ako PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ako RCSB], [https://www.ebi.ac.uk/pdbsum/6ako PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ako ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/FOXC2_HUMAN FOXC2_HUMAN] Defects in FOXC2 are the cause of lymphedema hereditary type 2 (LMPH2) [MIM:[https://omim.org/entry/153200 153200]; also known as Meige lymphedema. Hereditary lymphedema is a chronic disabling condition which results in swelling of the extremities due to altered lymphatic flow. Patients with lymphedema suffer from recurrent local infections, and physical impairment.<ref>PMID:11078474</ref> Defects in FOXC2 are a cause of lymphedema-yellow nails (LYYN) [MIM:[https://omim.org/entry/153300 153300]. LYYN is characterized by yellow, dystrophic, thick and slowly growing nails, associated with lymphedema and respiratory involvement. Lymphedema occurs more often in the lower limbs. It can appear at birth or later in life. Onset generally follows the onset of ungual abnormalities. Defects in FOXC2 are a cause of lymphedema-distichiasis (LYD) [MIM:[https://omim.org/entry/153400 153400]. LYD is characterized by primary limb lymphedema usually starting at puberty (but in some cases later or at birth) and associated with distichiasis (double rows of eyelashes, with extra eyelashes growing from the Meibomian gland orifices).<ref>PMID:11499682</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FOXC2_HUMAN FOXC2_HUMAN] Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.<ref>PMID:9169153</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The FOXC family of transcription factors (FOXC1 and FOXC2) plays essential roles in the regulation of embryonic, ocular, and cardiac development. Mutations and abnormal expression of FOXC proteins are implicated in genetic diseases as well as cancer. In this study, we determined two crystal structures of the DNA-binding domain (DBD) of human FOXC2 protein, in complex with different DNA sites. The FOXC2-DBD adopts the winged-helix fold with helix H3 contributing to all the base specific contacts, while the N-terminus, wing 1, and the C-terminus of FOXC2-DBD all make additional contacts with the phosphate groups of DNA. Our structural, biochemical, and bioinformatics analyses allow us to revise the previously proposed DNA recognition mechanism and provide a model of DNA binding for the FOXC proteins. In addition, our structural analysis and accompanying biochemical assays provide a molecular basis for understanding disease-causing mutations in FOXC1 and FOXC2.
-
Authors: Chen, X., Wei, H., Li, J., Liang, X., Dai, S., Jiang, L., Guo, M., Chen, Y.
+
Structural basis for DNA recognition by FOXC2.,Chen X, Wei H, Li J, Liang X, Dai S, Jiang L, Guo M, Qu L, Chen Z, Chen L, Chen Y Nucleic Acids Res. 2019 Feb 5. pii: 5306577. doi: 10.1093/nar/gkz077. PMID:30722065<ref>PMID:30722065</ref>
-
Description: Crystal Structure of FOXC2 DBD Bound to DBE2 DNA
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Guo, M]]
+
<div class="pdbe-citations 6ako" style="background-color:#fffaf0;"></div>
-
[[Category: Liang, X]]
+
 
-
[[Category: Jiang, L]]
+
==See Also==
-
[[Category: Chen, X]]
+
*[[FOX 3D structures|FOX 3D structures]]
-
[[Category: Dai, S]]
+
== References ==
-
[[Category: Li, J]]
+
<references/>
-
[[Category: Wei, H]]
+
__TOC__
-
[[Category: Chen, Y]]
+
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Chen X]]
 +
[[Category: Chen Y]]
 +
[[Category: Dai S]]
 +
[[Category: Guo M]]
 +
[[Category: Jiang L]]
 +
[[Category: Li J]]
 +
[[Category: Liang X]]
 +
[[Category: Wei H]]

Current revision

Crystal Structure of FOXC2 DBD Bound to DBE2 DNA

PDB ID 6ako

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools