2ilr

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of human Fanconi Anemia protein E C-terminal domain

Structural highlights

2ilr is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

FANCE_HUMAN Defects in FANCE are a cause of Fanconi anemia complementation group E (FANCE) [MIM:600901. A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.^[1]

Function

FANCE_HUMAN As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2.^[2] ^[3]

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

Fanconi Anaemia (FA) is a cancer predisposition disorder characterized by spontaneous chromosome breakage and high cellular sensitivity to genotoxic agents. In response to DNA damage, a multi-subunit assembly of FA proteins, the FA core complex, monoubiquitinates the downstream FANCD2 protein. The FANCE protein plays an essential role in the FA process of DNA repair as the FANCD2-binding component of the FA core complex. Here we report a crystallographic and biological study of human FANCE. The first structure of a FA protein reveals the presence of a repeated helical motif that provides a template for the structural rationalization of other proteins defective in Fanconi Anaemia. The portion of FANCE defined by our crystallographic analysis is sufficient for interaction with FANCD2, yielding structural information into the mode of FANCD2 recruitment to the FA core complex. Disease-associated mutations disrupt the FANCE-FANCD2 interaction, providing structural insight into the molecular mechanisms of FA pathogenesis.

Insights into Fanconi Anaemia from the structure of human FANCE.,Nookala RK, Hussain S, Pellegrini L Nucleic Acids Res. 2007;35(5):1638-48. Epub 2007 Feb 18. PMID:17308347^[4]

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

References

↑ de Winter JP, Leveille F, van Berkel CG, Rooimans MA, van Der Weel L, Steltenpool J, Demuth I, Morgan NV, Alon N, Bosnoyan-Collins L, Lightfoot J, Leegwater PA, Waisfisz Q, Komatsu K, Arwert F, Pronk JC, Mathew CG, Digweed M, Buchwald M, Joenje H. Isolation of a cDNA representing the Fanconi anemia complementation group E gene. Am J Hum Genet. 2000 Nov;67(5):1306-8. Epub 2000 Sep 19. PMID:11001585 doi:S0002-9297(07)62959-0
↑ Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ. FANCE: the link between Fanconi anaemia complex assembly and activity. EMBO J. 2002 Jul 1;21(13):3414-23. PMID:12093742 doi:10.1093/emboj/cdf355
↑ Wang X, Kennedy RD, Ray K, Stuckert P, Ellenberger T, D'Andrea AD. Chk1-mediated phosphorylation of FANCE is required for the Fanconi anemia/BRCA pathway. Mol Cell Biol. 2007 Apr;27(8):3098-108. Epub 2007 Feb 12. PMID:17296736 doi:10.1128/MCB.02357-06
↑ Nookala RK, Hussain S, Pellegrini L. Insights into Fanconi Anaemia from the structure of human FANCE. Nucleic Acids Res. 2007;35(5):1638-48. Epub 2007 Feb 18. PMID:17308347 doi:10.1093/nar/gkm033

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ilr"

Categories: Homo sapiens | Large Structures | Nookala RK | Pellegrini L

@@ Line 1: / Line 1: @@
 ==Crystal structure of human Fanconi Anemia protein E C-terminal domain==
-<StructureSection load='2ilr' size='340' side='right' caption='[[2ilr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='2ilr' size='340' side='right'caption='[[2ilr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ilr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ILR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ilr]] is a 1 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=2ILR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ILR FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FANCE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</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&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ilr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ilr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ilr RCSB], [http://www.ebi.ac.uk/pdbsum/2ilr PDBsum]</span></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=2ilr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ilr OCA], [https://pdbe.org/2ilr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ilr RCSB], [https://www.ebi.ac.uk/pdbsum/2ilr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ilr ProSAT]</span></td></tr>
-<table>
+</table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/FANCE_HUMAN FANCE_HUMAN]] Defects in FANCE are a cause of Fanconi anemia complementation group E (FANCE) [MIM:[http://omim.org/entry/600901 600901]]. A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.<ref>PMID:11001585</ref>
+[https://www.uniprot.org/uniprot/FANCE_HUMAN FANCE_HUMAN] Defects in FANCE are a cause of Fanconi anemia complementation group E (FANCE) [MIM:[https://omim.org/entry/600901 600901]. A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.<ref>PMID:11001585</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/FANCE_HUMAN FANCE_HUMAN]] As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2.<ref>PMID:12093742</ref> <ref>PMID:17296736</ref>
+[https://www.uniprot.org/uniprot/FANCE_HUMAN FANCE_HUMAN] As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2.<ref>PMID:12093742</ref> <ref>PMID:17296736</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/2ilr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/2ilr_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ilr ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ilr" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 33: / Line 35: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Nookala, R K.]]
+[[Category: Large Structures]]
-[[Category: Pellegrini, L.]]
+[[Category: Nookala RK]]
-[[Category: Antiparallel helical hairpin]]
+[[Category: Pellegrini L]]
-[[Category: Fanc repeat]]
-[[Category: Helical repeat]]
-[[Category: Oncoprotein]]

2ilr

From Proteopedia

Current revision

Crystal structure of human Fanconi Anemia protein E C-terminal domain

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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