1imt: Difference between revisions

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

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

caption="1imt" />

'''MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES'''<br />

==Overview==

The solution structure of mamba intestinal toxin 1 (MIT1), isolated from, Dendroaspis polylepis polylepis venom, has been determined. This molecule, is a cysteine-rich polypeptide exhibiting no recognised family membership., Resistance to MIT1 to classical specific endoproteases produced, contradictory NMR and biochemical information concerning disulphide-bridge, topology. We have used distance restraints allowing ambiguous partners, between S atoms in combination with NMR-derived structural information, to, correctly determine the disulphide-bridge topology. The resultant solution, structure of MIT1, determined to a resolution of 0.5 A, reveals an, unexpectedly similar global fold with respect to colipase, a protein, involved in fatty acid digestion. Colipase exhibits an analogous, resistance to endoprotease activity, indicating for the first time the, possible topological origins of this biochemical property. The biochemical, and structural homology permitted us to propose a mechanically related, digestive function for MIT1 and provides novel information concerning, snake venom protein evolution.

The solution structure of mamba intestinal toxin 1 (MIT1), isolated from Dendroaspis polylepis polylepis venom, has been determined. This molecule is a cysteine-rich polypeptide exhibiting no recognised family membership. Resistance to MIT1 to classical specific endoproteases produced contradictory NMR and biochemical information concerning disulphide-bridge topology. We have used distance restraints allowing ambiguous partners between S atoms in combination with NMR-derived structural information, to correctly determine the disulphide-bridge topology. The resultant solution structure of MIT1, determined to a resolution of 0.5 A, reveals an unexpectedly similar global fold with respect to colipase, a protein involved in fatty acid digestion. Colipase exhibits an analogous resistance to endoprotease activity, indicating for the first time the possible topological origins of this biochemical property. The biochemical and structural homology permitted us to propose a mechanically related digestive function for MIT1 and provides novel information concerning snake venom protein evolution.

==About this Structure==

1IMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1IMT OCA].

1IMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMT OCA].

==Reference==

Line 13:

[[Category: Dendroaspis polylepis polylepis]]

[[Category: Single protein]]

[[Category: Albrand, J.P.]]

[[Category: Albrand, J P.]]

[[Category: Blackledge, M.]]

[[Category: Boisbouvier, J.]]

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[[Category: venom]]

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@@ Line 1: / Line 1: @@
-[[Image:1imt.gif|left|200px]]<br /><applet load="1imt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1imt.gif|left|200px]]<br /><applet load="1imt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1imt" />
 '''MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES'''<br />
 ==Overview==
-The solution structure of mamba intestinal toxin 1 (MIT1), isolated from, Dendroaspis polylepis polylepis venom, has been determined. This molecule, is a cysteine-rich polypeptide exhibiting no recognised family membership., Resistance to MIT1 to classical specific endoproteases produced, contradictory NMR and biochemical information concerning disulphide-bridge, topology. We have used distance restraints allowing ambiguous partners, between S atoms in combination with NMR-derived structural information, to, correctly determine the disulphide-bridge topology. The resultant solution, structure of MIT1, determined to a resolution of 0.5 A, reveals an, unexpectedly similar global fold with respect to colipase, a protein, involved in fatty acid digestion. Colipase exhibits an analogous, resistance to endoprotease activity, indicating for the first time the, possible topological origins of this biochemical property. The biochemical, and structural homology permitted us to propose a mechanically related, digestive function for MIT1 and provides novel information concerning, snake venom protein evolution.
+The solution structure of mamba intestinal toxin 1 (MIT1), isolated from Dendroaspis polylepis polylepis venom, has been determined. This molecule is a cysteine-rich polypeptide exhibiting no recognised family membership. Resistance to MIT1 to classical specific endoproteases produced contradictory NMR and biochemical information concerning disulphide-bridge topology. We have used distance restraints allowing ambiguous partners between S atoms in combination with NMR-derived structural information, to correctly determine the disulphide-bridge topology. The resultant solution structure of MIT1, determined to a resolution of 0.5 A, reveals an unexpectedly similar global fold with respect to colipase, a protein involved in fatty acid digestion. Colipase exhibits an analogous resistance to endoprotease activity, indicating for the first time the possible topological origins of this biochemical property. The biochemical and structural homology permitted us to propose a mechanically related digestive function for MIT1 and provides novel information concerning snake venom protein evolution.
 ==About this Structure==
-IMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IMT OCA].
+IMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMT OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Dendroaspis polylepis polylepis]]
 [[Category: Single protein]]
-[[Category: Albrand, J.P.]]
+[[Category: Albrand, J P.]]
 [[Category: Blackledge, M.]]
 [[Category: Boisbouvier, J.]]
@@ Line 26: / Line 26: @@
 [[Category: venom]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:30:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:27 2008''