1SB2

High resolution Structure determination of rhodocetin

Summary for 1SB2

• Entry DOI: 10.2210/pdb1sb2/pdb
• Descriptor: Rhodocetin alpha subunit, Rhodocetin beta subunit (3 entities in total)
• Functional Keywords: c-type lectin; domain swapping, toxin
• Biological source: Calloselasma rhodostoma (Malayan pit viper); More
• Cellular location: Secreted: P81397 P81398
• Total number of polymer chains: 2
• Total formula weight: 31196.36

Authors

Paaventhan, P.,Kong, C.G.,Joseph, J.S.,Chung, M.C.M.,Kolatkar, P.R. (deposition date: 2004-02-10, release date: 2005-02-01, Last modification date: 2024-10-16)

Primary citation

Paaventhan, P.,Kong, C.G.,Joseph, J.S.,Chung, M.C.M.,Kolatkar, P.R.
Structure of rhodocetin reveals noncovalently bound heterodimer interface
Protein Sci., 14:169-175, 2005

PubMed Abstract: 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.

PubMed: 15576563
DOI: 10.1110/ps.04945605

Experimental method

X-RAY DIFFRACTION (1.9 Å)