1sb2: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sb2 OCA], [http://www.ebi.ac.uk/pdbsum/1sb2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sb2 RCSB]</span> | |||
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[[Category: Kong, C G.]] | [[Category: Kong, C G.]] | ||
[[Category: Paaventhan, P.]] | [[Category: Paaventhan, P.]] | ||
[[Category: c-type lectin | [[Category: c-type lectin]] | ||
[[Category: domain swapping]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:39:44 2008'' | ||
Revision as of 23:39, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
High resolution Structure determination of rhodocetin
OverviewOverview
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.
About this StructureAbout this Structure
1SB2 is a Protein complex structure of sequences from Calloselasma rhodostoma. Full crystallographic information is available from OCA.
ReferenceReference
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
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