1sb2: Difference between revisions

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[[Image:1sb2.gif|left|200px]]<br /><applet load="1sb2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1sb2.gif|left|200px]]<br /><applet load="1sb2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1sb2, resolution 1.90Å" />

'''High resolution Structure determination of rhodocetin'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1SB2 OCA].

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==

Line 13:

[[Category: Calloselasma rhodostoma]]

[[Category: Protein complex]]

[[Category: Chung, M.C.M.]]

[[Category: Chung, M C.M.]]

[[Category: Joseph, J.S.]]

[[Category: Joseph, J S.]]

[[Category: Kolatkar, P.R.]]

[[Category: Kolatkar, P R.]]

[[Category: Kong, C.G.]]

[[Category: Kong, C G.]]

[[Category: Paaventhan, P.]]

[[Category: c-type lectin; domain swapping]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:14:~~23 2007~~''

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@@ Line 1: / Line 1: @@
-[[Image:1sb2.gif|left|200px]]<br /><applet load="1sb2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1sb2.gif|left|200px]]<br /><applet load="1sb2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1sb2, resolution 1.90&Aring;" />
 '''High resolution Structure determination of rhodocetin'''<br />
 ==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.
+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==
-SB2 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SB2 OCA].
+SB2 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==
@@ Line 13: / Line 13: @@
 [[Category: Calloselasma rhodostoma]]
 [[Category: Protein complex]]
-[[Category: Chung, M.C.M.]]
+[[Category: Chung, M C.M.]]
-[[Category: Joseph, J.S.]]
+[[Category: Joseph, J S.]]
-[[Category: Kolatkar, P.R.]]
+[[Category: Kolatkar, P R.]]
-[[Category: Kong, C.G.]]
+[[Category: Kong, C G.]]
 [[Category: Paaventhan, P.]]
 [[Category: c-type lectin; domain swapping]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:14:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:40 2008''