4xcr

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'''Unreleased structure'''
 
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The entry 4xcr is ON HOLD
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==Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant I35A==
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<StructureSection load='4xcr' size='340' side='right'caption='[[4xcr]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xcr]] 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=4XCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XCR 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]] 3.602&#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=4xcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xcr OCA], [https://pdbe.org/4xcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xcr RCSB], [https://www.ebi.ac.uk/pdbsum/4xcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xcr ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[https://omim.org/entry/105400 105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. 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 cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Although protein folding and stability have been well explored under simplified conditions in vitro, it is yet unclear how these basic self-organization events are modulated by the crowded interior of live cells. To find out, we use here in-cell NMR to follow at atomic resolution the thermal unfolding of a beta-barrel protein inside mammalian and bacterial cells. Challenging the view from in vitro crowding effects, we find that the cells destabilize the protein at 37 degrees C but with a conspicuous twist: While the melting temperature goes down the cold unfolding moves into the physiological regime, coupled to an augmented heat-capacity change. The effect seems induced by transient, sequence-specific, interactions with the cellular components, acting preferentially on the unfolded ensemble. This points to a model where the in vivo influence on protein behavior is case specific, determined by the individual protein's interplay with the functionally optimized "interaction landscape" of the cellular interior.
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Authors: Wang, H., Logan, D.T., Danielsson, J., Mu, X., Binolfi, A., Theillet, F., Bekei, B., Lang, L., Wennerstrom, H., Selenko, P., Oliveberg, M.
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Thermodynamics of protein destabilization in live cells.,Danielsson J, Mu X, Lang L, Wang H, Binolfi A, Theillet FX, Bekei B, Logan DT, Selenko P, Wennerstrom H, Oliveberg M Proc Natl Acad Sci U S A. 2015 Oct 6;112(40):12402-7. doi:, 10.1073/pnas.1511308112. Epub 2015 Sep 21. PMID:26392565<ref>PMID:26392565</ref>
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Description: Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant I35A
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Logan, D.T]]
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<div class="pdbe-citations 4xcr" style="background-color:#fffaf0;"></div>
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[[Category: Wennerstrom, H]]
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[[Category: Selenko, P]]
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==See Also==
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[[Category: Theillet, F]]
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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[[Category: Oliveberg, M]]
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== References ==
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[[Category: Mu, X]]
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<references/>
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[[Category: Danielsson, J]]
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__TOC__
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[[Category: Binolfi, A]]
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</StructureSection>
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[[Category: Wang, H]]
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[[Category: Homo sapiens]]
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[[Category: Lang, L]]
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[[Category: Large Structures]]
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[[Category: Bekei, B]]
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[[Category: Bekei B]]
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[[Category: Binolfi A]]
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[[Category: Danielsson J]]
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[[Category: Lang L]]
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[[Category: Logan DT]]
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[[Category: Mu X]]
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[[Category: Oliveberg M]]
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[[Category: Selenko P]]
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[[Category: Theillet F]]
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[[Category: Wang H]]
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[[Category: Wennerstrom H]]

Current revision

Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant I35A

PDB ID 4xcr

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