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https://doi.org/10.1110/ps.04945605
DC Field | Value | |
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dc.title | Structure of rhodocetin reveals noncovalently bound heterodimer interface | |
dc.contributor.author | Paaventhan, P. | |
dc.contributor.author | Kong, C. | |
dc.contributor.author | Joseph, J.S. | |
dc.contributor.author | Chung, M.C.M. | |
dc.contributor.author | Kolatkar, P.R. | |
dc.date.accessioned | 2016-11-16T11:05:37Z | |
dc.date.available | 2016-11-16T11:05:37Z | |
dc.date.issued | 2005-01 | |
dc.identifier.citation | Paaventhan, 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.issn | 09618368 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/130407 | |
dc.description.abstract | Rhodocetin 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.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1110/ps.04945605 | |
dc.source | Scopus | |
dc.subject | C-type lectin-like protein | |
dc.subject | Calloselasma rhodostoma | |
dc.subject | Domain swapping | |
dc.subject | Heterodimer | |
dc.subject | Platelet aggregation inhibitor | |
dc.type | Article | |
dc.contributor.department | BIOCHEMISTRY | |
dc.contributor.department | BIOLOGICAL SCIENCES | |
dc.description.doi | 10.1110/ps.04945605 | |
dc.description.sourcetitle | Protein Science | |
dc.description.volume | 14 | |
dc.description.issue | 1 | |
dc.description.page | 169-175 | |
dc.description.coden | PRCIE | |
dc.identifier.isiut | 000226384300018 | |
Appears in Collections: | Staff Publications |
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