Structural highlights
Function
[SLEA_CALRH] Potent inhibitor of collagen-induced platelet aggregation. It acts by binding to the integrin alpha2A domain and blocks collagen binding to integrin alpha-2/beta-1 (ITGA2/ITGB1). The gamma/delta subunits mainly contribute to this activity.[1] [2] [3] [SLEB_CALRH] Potent inhibitor of collagen-induced platelet aggregation. It acts by binding to the integrin alpha2A domain and blocks collagen binding to integrin alpha-2/beta-1 (ITGA2/ITGB1). The gamma/delta subunits mainly contribute to this activity.[4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Rhodocetin is a unique heterodimer consisting of alpha- and beta-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 Ca(2+)-dependent lectin-like proteins. We report here the 1.9 A resolution structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity.
Structure of rhodocetin reveals noncovalently bound heterodimer interface.,Paaventhan P, Kong C, Joseph JS, Chung MC, Kolatkar PR Protein Sci. 2005 Jan;14(1):169-75. Epub 2004 Dec 2. PMID:15576563[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang R, Kini RM, Chung MC. Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): synergistic and noncovalent interaction between its subunits. Biochemistry. 1999 Jun 8;38(23):7584-93. PMID:10360956 doi:http://dx.doi.org/10.1021/bi982132z
- ↑ Eble JA, Beermann B, Hinz HJ, Schmidt-Hederich A. alpha 2beta 1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen. J Biol Chem. 2001 Apr 13;276(15):12274-84. Epub 2000 Dec 19. PMID:11121411 doi:http://dx.doi.org/10.1074/jbc.M009338200
- ↑ Eble JA, Tuckwell DS. The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the integrin alpha2 subunit proximal to the collagen-binding site. Biochem J. 2003 Nov 15;376(Pt 1):77-85. PMID:12871211 doi:http://dx.doi.org/10.1042/BJ20030373
- ↑ Wang R, Kini RM, Chung MC. Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): synergistic and noncovalent interaction between its subunits. Biochemistry. 1999 Jun 8;38(23):7584-93. PMID:10360956 doi:http://dx.doi.org/10.1021/bi982132z
- ↑ Eble JA, Beermann B, Hinz HJ, Schmidt-Hederich A. alpha 2beta 1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen. J Biol Chem. 2001 Apr 13;276(15):12274-84. Epub 2000 Dec 19. PMID:11121411 doi:http://dx.doi.org/10.1074/jbc.M009338200
- ↑ Eble JA, Tuckwell DS. The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the integrin alpha2 subunit proximal to the collagen-binding site. Biochem J. 2003 Nov 15;376(Pt 1):77-85. PMID:12871211 doi:http://dx.doi.org/10.1042/BJ20030373
- ↑ Paaventhan P, Kong C, Joseph JS, Chung MC, Kolatkar PR. Structure of rhodocetin reveals noncovalently bound heterodimer interface. Protein Sci. 2005 Jan;14(1):169-75. Epub 2004 Dec 2. PMID:15576563 doi:http://dx.doi.org/10.1110/ps.04945605
