5xsg
From Proteopedia
(Difference between revisions)
m (Protected "5xsg" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Ultrahigh resolution structure of FUS (37-42) SYSGYS determined by MicroED== |
| - | + | <StructureSection load='5xsg' size='340' side='right' caption='[[5xsg]], [[Resolution|resolution]] 0.73Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5xsg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XSG FirstGlance]. <br> | |
| - | + | </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=5xsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xsg OCA], [http://pdbe.org/5xsg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xsg RCSB], [http://www.ebi.ac.uk/pdbsum/5xsg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xsg ProSAT]</span></td></tr> | |
| - | [[Category: | + | </table> |
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/FUS_HUMAN FUS_HUMAN]] Frontotemporal dementia with motor neuron disease;Hereditary essential tremor;Amyotrophic lateral sclerosis;Juvenile amyotrophic lateral sclerosis;Myxofibrosarcoma;Myxoid/round cell liposarcoma. A chromosomal aberration involving FUS is found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with DDIT3. A chromosomal aberration involving FUS is a cause of acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with ERG. The disease may be caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving FUS is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(12;16)(q13;p11.2) with ATF1 generates a chimeric FUS/ATF1 protein. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FUS_HUMAN FUS_HUMAN]] Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gui, X]] | ||
| + | [[Category: Li, D]] | ||
| + | [[Category: Li, X]] | ||
| + | [[Category: Liu, C]] | ||
| + | [[Category: Luo, F]] | ||
| + | [[Category: Zhou, H]] | ||
| + | [[Category: Cross-coil amyloid fibril]] | ||
| + | [[Category: Fus low complexity domain]] | ||
| + | [[Category: Reversible amyloid fibril]] | ||
| + | [[Category: Rna binding protein]] | ||
| + | [[Category: Rna granule assembly]] | ||
Revision as of 05:55, 4 April 2018
Ultrahigh resolution structure of FUS (37-42) SYSGYS determined by MicroED
| |||||||||||
