Structure of rhodocetin reveals noncovalently bound heterodimer interface

Palasingam Paaventhan; Chunguang Kong; Jeremiah S. Joseph; Max C.M. Chung; Prasanna R. Kolatkar

doi:10.1110/ps.04945605

Structure of rhodocetin reveals noncovalently bound heterodimer interface

Palasingam Paaventhan, Chunguang Kong, Jeremiah S. Joseph, Max C.M. Chung, Prasanna R. Kolatkar^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

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.

Original language	English
Pages (from-to)	169-175
Number of pages	7
Journal	Protein Science
Volume	14
Issue number	1
DOIs	https://doi.org/10.1110/ps.04945605
Publication status	Published - Jan 2005
Externally published	Yes

Keywords

C-type lectin-like protein
Calloselasma rhodostoma
Domain swapping
Heterodimer
Platelet aggregation inhibitor

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title = "Structure of rhodocetin reveals noncovalently bound heterodimer interface",

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 {\AA} resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity.",

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doi = "10.1110/ps.04945605",

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journal = "Protein Science",

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AU - Paaventhan, Palasingam

AU - Kong, Chunguang

AU - Joseph, Jeremiah S.

AU - Chung, Max C.M.

AU - Kolatkar, Prasanna R.

PY - 2005/1

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N2 - 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.

AB - 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.

KW - C-type lectin-like protein

KW - Calloselasma rhodostoma

KW - Domain swapping

KW - Heterodimer

KW - Platelet aggregation inhibitor

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M3 - Article

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AN - SCOPUS:11144233375

SN - 0961-8368

VL - 14

SP - 169

EP - 175

JO - Protein Science

JF - Protein Science

IS - 1

ER -

Structure of rhodocetin reveals noncovalently bound heterodimer interface

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Keywords

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