2bvb: Difference between revisions

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[[Image:2bvb.gif|left|200px]]<br /><applet load="2bvb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2bvb.gif|left|200px]]<br /><applet load="2bvb" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2bvb" />

'''THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII'''<br />

==Overview==

Immediately prior to invasion Toxoplasma gondii tachyzoites release a, large number of micronemal proteins (TgMICs) that participate in host cell, attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to, be identified in T. gondii and has been recently shown to be critical in, invasion. This study establishes that the N-terminal thrombospondin type I, repeat-like domains (TSR1-like) from TgMIC1 function as an independent, adhesin as well as promoting association with TgMIC4. Using the newly, solved three-dimensional structure of the C-terminal domain of TgMIC1 we, have identified a novel Galectin-like fold that does not possess, carbohydrate binding properties and redefines the architecture of TgMIC1., Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism, for successful exit from the early secretory compartments and for, subsequent trafficking of the complex to the micronemes.

Immediately prior to invasion Toxoplasma gondii tachyzoites release a large number of micronemal proteins (TgMICs) that participate in host cell attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to be identified in T. gondii and has been recently shown to be critical in invasion. This study establishes that the N-terminal thrombospondin type I repeat-like domains (TSR1-like) from TgMIC1 function as an independent adhesin as well as promoting association with TgMIC4. Using the newly solved three-dimensional structure of the C-terminal domain of TgMIC1 we have identified a novel Galectin-like fold that does not possess carbohydrate binding properties and redefines the architecture of TgMIC1. Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism for successful exit from the early secretory compartments and for subsequent trafficking of the complex to the micronemes.

==About this Structure==

2BVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA].

2BVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA].

==Reference==

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[[Category: microneme]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 08:56:01 ~~2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:01 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2bvb.gif|left|200px]]<br /><applet load="2bvb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bvb.gif|left|200px]]<br /><applet load="2bvb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bvb" />
 '''THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA GONDII'''<br />
 ==Overview==
-Immediately prior to invasion Toxoplasma gondii tachyzoites release a, large number of micronemal proteins (TgMICs) that participate in host cell, attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to, be identified in T. gondii and has been recently shown to be critical in, invasion. This study establishes that the N-terminal thrombospondin type I, repeat-like domains (TSR1-like) from TgMIC1 function as an independent, adhesin as well as promoting association with TgMIC4. Using the newly, solved three-dimensional structure of the C-terminal domain of TgMIC1 we, have identified a novel Galectin-like fold that does not possess, carbohydrate binding properties and redefines the architecture of TgMIC1., Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism, for successful exit from the early secretory compartments and for, subsequent trafficking of the complex to the micronemes.
+Immediately prior to invasion Toxoplasma gondii tachyzoites release a large number of micronemal proteins (TgMICs) that participate in host cell attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to be identified in T. gondii and has been recently shown to be critical in invasion. This study establishes that the N-terminal thrombospondin type I repeat-like domains (TSR1-like) from TgMIC1 function as an independent adhesin as well as promoting association with TgMIC4. Using the newly solved three-dimensional structure of the C-terminal domain of TgMIC1 we have identified a novel Galectin-like fold that does not possess carbohydrate binding properties and redefines the architecture of TgMIC1. Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism for successful exit from the early secretory compartments and for subsequent trafficking of the complex to the micronemes.
 ==About this Structure==
-BVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA].
+BVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA].
 ==Reference==
@@ Line 30: / Line 30: @@
 [[Category: microneme]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:56:01 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:01 2008''