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

Access to Document

10.1110/ps.04945605

Cite this

@article{53e0679e2d664e1cb6aa2f0c904ec9f4,

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.",

keywords = "C-type lectin-like protein, Calloselasma rhodostoma, Domain swapping, Heterodimer, Platelet aggregation inhibitor",

author = "Palasingam Paaventhan and Chunguang Kong and Joseph, \{Jeremiah S.\} and Chung, \{Max C.M.\} and Kolatkar, \{Prasanna R.\}",

year = "2005",

month = jan,

doi = "10.1110/ps.04945605",

language = "English",

volume = "14",

pages = "169--175",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Wiley-Blackwell",

number = "1",

}

TY - JOUR

T1 - Structure of rhodocetin reveals noncovalently bound heterodimer interface

AU - Paaventhan, Palasingam

AU - Kong, Chunguang

AU - Joseph, Jeremiah S.

AU - Chung, Max C.M.

AU - Kolatkar, Prasanna R.

PY - 2005/1

Y1 - 2005/1

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

UR - https://www.scopus.com/pages/publications/11144233375

U2 - 10.1110/ps.04945605

DO - 10.1110/ps.04945605

M3 - Article

C2 - 15576563

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this