1sb2
From Proteopedia
(New page: 200px<br /><applet load="1sb2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sb2, resolution 1.90Å" /> '''High resolution Stru...) |
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| - | [[Image:1sb2.gif|left|200px]]<br /><applet load="1sb2" size=" | + | [[Image:1sb2.gif|left|200px]]<br /><applet load="1sb2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sb2, resolution 1.90Å" /> | caption="1sb2, resolution 1.90Å" /> | ||
'''High resolution Structure determination of rhodocetin'''<br /> | '''High resolution Structure determination of rhodocetin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rhodocetin is a unique heterodimer consisting of alpha- and beta-subunits | + | 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 Structure== | ==About this Structure== | ||
| - | 1SB2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma]. Full crystallographic information is available from [http:// | + | 1SB2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SB2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Calloselasma rhodostoma]] | [[Category: Calloselasma rhodostoma]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Chung, M | + | [[Category: Chung, M C.M.]] |
| - | [[Category: Joseph, J | + | [[Category: Joseph, J S.]] |
| - | [[Category: Kolatkar, P | + | [[Category: Kolatkar, P R.]] |
| - | [[Category: Kong, C | + | [[Category: Kong, C G.]] |
[[Category: Paaventhan, P.]] | [[Category: Paaventhan, P.]] | ||
[[Category: c-type lectin; domain swapping]] | [[Category: c-type lectin; domain swapping]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:40 2008'' |
Revision as of 12:59, 21 February 2008
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High resolution Structure determination of rhodocetin
Overview
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 Structure
1SB2 is a Protein complex structure of sequences from Calloselasma rhodostoma. Full crystallographic information is available from OCA.
Reference
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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