2p22: Difference between revisions

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==Overview==

The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation, of ubiquitinated transmembrane proteins and the budding of the HIV virus., Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The, crystal structure of the heterotetrameric ESCRT-I complex reveals a highly, asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is, nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk., The stalk is important for cargo sorting by ESCRT-I and is proposed to, serve as a spacer regulating the correct disposition of cargo and other, ESCRT components. Hydrodynamic constraints and crystallographic structures, were used to generate a model of intact ESCRT-I in solution. The results, show how ESCRT-I uses a combination of a rigid stalk and flexible tethers, to interact with lipids, cargo, and other ESCRT complexes over a span of, approximately 25 nm.

The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation of ubiquitinated transmembrane proteins and the budding of the HIV virus. Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The crystal structure of the heterotetrameric ESCRT-I complex reveals a highly asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk. The stalk is important for cargo sorting by ESCRT-I and is proposed to serve as a spacer regulating the correct disposition of cargo and other ESCRT components. Hydrodynamic constraints and crystallographic structures were used to generate a model of intact ESCRT-I in solution. The results show how ESCRT-I uses a combination of a rigid stalk and flexible tethers to interact with lipids, cargo, and other ESCRT complexes over a span of approximately 25 nm.

==About this Structure==

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[[Category: Protein complex]]

[[Category: Saccharomyces cerevisiae]]

[[Category: Hurley, J.H.]]

[[Category: Hurley, J H.]]

[[Category: Kostelansky, MS]]

[[Category: SO4]]

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[[Category: vps37]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation, of ubiquitinated transmembrane proteins and the budding of the HIV virus., Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The, crystal structure of the heterotetrameric ESCRT-I complex reveals a highly, asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is, nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk., The stalk is important for cargo sorting by ESCRT-I and is proposed to, serve as a spacer regulating the correct disposition of cargo and other, ESCRT components. Hydrodynamic constraints and crystallographic structures, were used to generate a model of intact ESCRT-I in solution. The results, show how ESCRT-I uses a combination of a rigid stalk and flexible tethers, to interact with lipids, cargo, and other ESCRT complexes over a span of, approximately 25 nm.
+The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation of ubiquitinated transmembrane proteins and the budding of the HIV virus. Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The crystal structure of the heterotetrameric ESCRT-I complex reveals a highly asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk. The stalk is important for cargo sorting by ESCRT-I and is proposed to serve as a spacer regulating the correct disposition of cargo and other ESCRT components. Hydrodynamic constraints and crystallographic structures were used to generate a model of intact ESCRT-I in solution. The results show how ESCRT-I uses a combination of a rigid stalk and flexible tethers to interact with lipids, cargo, and other ESCRT complexes over a span of approximately 25 nm.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Hurley, J.H.]]
+[[Category: Hurley, J H.]]
 [[Category: Kostelansky, MS]]
 [[Category: SO4]]
@@ Line 29: / Line 29: @@
 [[Category: vps37]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:01:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:02 2008''