4x25

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(New page: '''Unreleased structure''' The entry 4x25 is ON HOLD until Paper Publication Authors: Silvas, T.V., Shandilya, S.M.D., Schiffer, C.A. Description: Profilin-1 M114T mutant: ALS-causing ...)
Current revision (12:59, 1 March 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4x25 is ON HOLD until Paper Publication
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==Structural basis for mutation-induced destabilization of Profilin 1 in ALS==
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<StructureSection load='4x25' size='340' side='right'caption='[[4x25]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4x25]] is a 2 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=4X25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X25 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4x25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x25 OCA], [https://pdbe.org/4x25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x25 RCSB], [https://www.ebi.ac.uk/pdbsum/4x25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x25 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[https://omim.org/entry/614808 614808]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.<ref>PMID:18573880</ref>
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Authors: Silvas, T.V., Shandilya, S.M.D., Schiffer, C.A.
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==See Also==
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*[[Profilin 3D Structures|Profilin 3D Structures]]
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Description: Profilin-1 M114T mutant: ALS-causing mutations destabilize the native conformation
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Schiffer CA]]
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[[Category: Shandilya SMD]]
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[[Category: Silvas TV]]

Current revision

Structural basis for mutation-induced destabilization of Profilin 1 in ALS

PDB ID 4x25

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