Please use this identifier to cite or link to this item: https://doi.org/10.1110/ps.04945605
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dc.titleStructure of rhodocetin reveals noncovalently bound heterodimer interface
dc.contributor.authorPaaventhan, P.
dc.contributor.authorKong, C.
dc.contributor.authorJoseph, J.S.
dc.contributor.authorChung, M.C.M.
dc.contributor.authorKolatkar, P.R.
dc.date.accessioned2016-11-16T11:05:37Z
dc.date.available2016-11-16T11:05:37Z
dc.date.issued2005-01
dc.identifier.citationPaaventhan, P., Kong, C., Joseph, J.S., Chung, M.C.M., Kolatkar, P.R. (2005-01). Structure of rhodocetin reveals noncovalently bound heterodimer interface. Protein Science 14 (1) : 169-175. ScholarBank@NUS Repository. https://doi.org/10.1110/ps.04945605
dc.identifier.issn09618368
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/130407
dc.description.abstractRhodocetin is a unique heterodimer consisting of α- and β-subunits of 133 and 129 residues, respectively. The molecule, purified from the crude venom of the Malayan pit viper, Calloselasma rhodostoma, functions as an inhibitor of collagen-induced aggregation. Rhodocetin has been shown to have activity only when present as a dimer. The dimer is formed without an intersubunit disulfide bridge, unlike all the other Ca2+- dependent lectin-like proteins. We report here the 1.9 Å resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1110/ps.04945605
dc.sourceScopus
dc.subjectC-type lectin-like protein
dc.subjectCalloselasma rhodostoma
dc.subjectDomain swapping
dc.subjectHeterodimer
dc.subjectPlatelet aggregation inhibitor
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1110/ps.04945605
dc.description.sourcetitleProtein Science
dc.description.volume14
dc.description.issue1
dc.description.page169-175
dc.description.codenPRCIE
dc.identifier.isiut000226384300018
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