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Article: Identification of allosteric disulfides from labile bonds in X-ray structures
Title | Identification of allosteric disulfides from labile bonds in X-ray structures |
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Authors | |
Keywords | Allosteric disulfides Coagulation Complement Oxygen-sensing Redox |
Issue Date | 2018 |
Publisher | The Royal Society Publishing: Open Access. The Journal's web site is located at http://rsos.royalsocietypublishing.org/ |
Citation | Royal Society Open Science, 2018, v. 5 n. 2, p. 171058 How to Cite? |
Abstract | Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed. Here, we identify potential allosteric disulfides in all Protein Data Bank X-ray structures from bonds that are present in some molecules of a protein crystal but absent in others, or present in some structures of a protein but absent in others. We reasoned that the labile nature of these disulfides signifies a propensity for cleavage and so possible allosteric regulation of the protein in which the bond resides. A total of 511 labile disulfide bonds were identified. The labile disulfides are more stressed than the average bond, being characterized by high average torsional strain and stretching of the sulfur-sulfur bond and neighbouring bond angles. This pre-stress likely underpins their susceptibility to cleavage. The coagulation, complement and oxygen-sensing hypoxia inducible factor-1 pathways, which are known or have been suggested to be regulated by allosteric disulfides, are enriched in proteins containing labile disulfides. The identification of labile disulfide bonds will facilitate the study of this post-translational modification. |
Persistent Identifier | http://hdl.handle.net/10722/267374 |
ISSN | 2023 Impact Factor: 2.9 2023 SCImago Journal Rankings: 0.787 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Pijning, AE | - |
dc.contributor.author | Chiu, J | - |
dc.contributor.author | Yeo, RX | - |
dc.contributor.author | Wong, WHJ | - |
dc.contributor.author | Hogg, PJ | - |
dc.date.accessioned | 2019-02-18T09:00:43Z | - |
dc.date.available | 2019-02-18T09:00:43Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Royal Society Open Science, 2018, v. 5 n. 2, p. 171058 | - |
dc.identifier.issn | 2054-5703 | - |
dc.identifier.uri | http://hdl.handle.net/10722/267374 | - |
dc.description.abstract | Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed. Here, we identify potential allosteric disulfides in all Protein Data Bank X-ray structures from bonds that are present in some molecules of a protein crystal but absent in others, or present in some structures of a protein but absent in others. We reasoned that the labile nature of these disulfides signifies a propensity for cleavage and so possible allosteric regulation of the protein in which the bond resides. A total of 511 labile disulfide bonds were identified. The labile disulfides are more stressed than the average bond, being characterized by high average torsional strain and stretching of the sulfur-sulfur bond and neighbouring bond angles. This pre-stress likely underpins their susceptibility to cleavage. The coagulation, complement and oxygen-sensing hypoxia inducible factor-1 pathways, which are known or have been suggested to be regulated by allosteric disulfides, are enriched in proteins containing labile disulfides. The identification of labile disulfide bonds will facilitate the study of this post-translational modification. | - |
dc.language | eng | - |
dc.publisher | The Royal Society Publishing: Open Access. The Journal's web site is located at http://rsos.royalsocietypublishing.org/ | - |
dc.relation.ispartof | Royal Society Open Science | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.subject | Allosteric disulfides | - |
dc.subject | Coagulation | - |
dc.subject | Complement | - |
dc.subject | Oxygen-sensing | - |
dc.subject | Redox | - |
dc.title | Identification of allosteric disulfides from labile bonds in X-ray structures | - |
dc.type | Article | - |
dc.identifier.email | Wong, WHJ: jwhwong@hku.hk | - |
dc.identifier.authority | Wong, WHJ=rp02363 | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1098/rsos.171058 | - |
dc.identifier.scopus | eid_2-s2.0-85042777882 | - |
dc.identifier.hkuros | 296866 | - |
dc.identifier.volume | 5 | - |
dc.identifier.issue | 2 | - |
dc.identifier.spage | 171058 | - |
dc.identifier.epage | 171058 | - |
dc.identifier.isi | WOS:000426465700016 | - |
dc.publisher.place | United Kingdom | - |
dc.identifier.issnl | 2054-5703 | - |