1bpv: Difference between revisions

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

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

caption="1bpv" />

'''TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES'''<br />

==Overview==

BACKGROUND: Titin is a huge protein ( approximately 3 MDa) that is present, in the contractile unit (sarcomere) of striated muscle and has a key role, in muscle assembly and elasticity. Titin is mainly composed of two types, of module (type I and II). Type I modules are found exclusively in the, region of titin localised in the A band, where they are arranged in a, super-repeat pattern that correlates with the ultrastructure of the thick, filament. No structure of a titin type I module has been reported so far., RESULTS: We have determined the structure of a representative type I, module, A71, using nuclear magnetic resonance (NMR) spectroscopy. The, structure has the predicted fibronectin type III fold. Titin-specific, conserved residues are either located at the putative module-module, interfaces or along one side of the protein surface. Several proline, residues that contribute to two stretches in a polyproline II helix, conformation are solvent-exposed and line up as a continuous ribbon, extending over more than two-thirds of the module surface. Homology models, of the type I module N-terminal to A71 (A70) and the double module A70-A71, were used to discuss possible intermodule interactions and their role in, module-module orientation. CONCLUSIONS: As residues at the module-module, interfaces are highly conserved, we speculate that similar interactions, govern all of the interfaces between type I modules in titin. This, conservation would lead to a regular multiple array of similar surface, structures. Such an arrangement would allow arrays of contiguous type I, modules to expose multiple proline stretches in a highly regular way and, these may act as binding sites for other thick filament proteins.

BACKGROUND: Titin is a huge protein ( approximately 3 MDa) that is present in the contractile unit (sarcomere) of striated muscle and has a key role in muscle assembly and elasticity. Titin is mainly composed of two types of module (type I and II). Type I modules are found exclusively in the region of titin localised in the A band, where they are arranged in a super-repeat pattern that correlates with the ultrastructure of the thick filament. No structure of a titin type I module has been reported so far. RESULTS: We have determined the structure of a representative type I module, A71, using nuclear magnetic resonance (NMR) spectroscopy. The structure has the predicted fibronectin type III fold. Titin-specific conserved residues are either located at the putative module-module interfaces or along one side of the protein surface. Several proline residues that contribute to two stretches in a polyproline II helix conformation are solvent-exposed and line up as a continuous ribbon extending over more than two-thirds of the module surface. Homology models of the type I module N-terminal to A71 (A70) and the double module A70-A71 were used to discuss possible intermodule interactions and their role in module-module orientation. CONCLUSIONS: As residues at the module-module interfaces are highly conserved, we speculate that similar interactions govern all of the interfaces between type I modules in titin. This conservation would lead to a regular multiple array of similar surface structures. Such an arrangement would allow arrays of contiguous type I modules to expose multiple proline stretches in a highly regular way and these may act as binding sites for other thick filament proteins.

==About this Structure==

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

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

==Reference==

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[[Category: titin]]

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@@ Line 1: / Line 1: @@
-[[Image:1bpv.gif|left|200px]]<br /><applet load="1bpv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1bpv.gif|left|200px]]<br /><applet load="1bpv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1bpv" />
 '''TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES'''<br />
 ==Overview==
-BACKGROUND: Titin is a huge protein ( approximately 3 MDa) that is present, in the contractile unit (sarcomere) of striated muscle and has a key role, in muscle assembly and elasticity. Titin is mainly composed of two types, of module (type I and II). Type I modules are found exclusively in the, region of titin localised in the A band, where they are arranged in a, super-repeat pattern that correlates with the ultrastructure of the thick, filament. No structure of a titin type I module has been reported so far., RESULTS: We have determined the structure of a representative type I, module, A71, using nuclear magnetic resonance (NMR) spectroscopy. The, structure has the predicted fibronectin type III fold. Titin-specific, conserved residues are either located at the putative module-module, interfaces or along one side of the protein surface. Several proline, residues that contribute to two stretches in a polyproline II helix, conformation are solvent-exposed and line up as a continuous ribbon, extending over more than two-thirds of the module surface. Homology models, of the type I module N-terminal to A71 (A70) and the double module A70-A71, were used to discuss possible intermodule interactions and their role in, module-module orientation. CONCLUSIONS: As residues at the module-module, interfaces are highly conserved, we speculate that similar interactions, govern all of the interfaces between type I modules in titin. This, conservation would lead to a regular multiple array of similar surface, structures. Such an arrangement would allow arrays of contiguous type I, modules to expose multiple proline stretches in a highly regular way and, these may act as binding sites for other thick filament proteins.
+BACKGROUND: Titin is a huge protein ( approximately 3 MDa) that is present in the contractile unit (sarcomere) of striated muscle and has a key role in muscle assembly and elasticity. Titin is mainly composed of two types of module (type I and II). Type I modules are found exclusively in the region of titin localised in the A band, where they are arranged in a super-repeat pattern that correlates with the ultrastructure of the thick filament. No structure of a titin type I module has been reported so far. RESULTS: We have determined the structure of a representative type I module, A71, using nuclear magnetic resonance (NMR) spectroscopy. The structure has the predicted fibronectin type III fold. Titin-specific conserved residues are either located at the putative module-module interfaces or along one side of the protein surface. Several proline residues that contribute to two stretches in a polyproline II helix conformation are solvent-exposed and line up as a continuous ribbon extending over more than two-thirds of the module surface. Homology models of the type I module N-terminal to A71 (A70) and the double module A70-A71 were used to discuss possible intermodule interactions and their role in module-module orientation. CONCLUSIONS: As residues at the module-module interfaces are highly conserved, we speculate that similar interactions govern all of the interfaces between type I modules in titin. This conservation would lead to a regular multiple array of similar surface structures. Such an arrangement would allow arrays of contiguous type I modules to expose multiple proline stretches in a highly regular way and these may act as binding sites for other thick filament proteins.
 ==About this Structure==
-BPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BPV OCA].
+BPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BPV OCA].
 ==Reference==
@@ Line 20: / Line 20: @@
 [[Category: titin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:49:24 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:48 2008''