1ya5
From Proteopedia
(New page: 200px<br /> <applet load="1ya5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ya5, resolution 2.445Å" /> '''Crystal structure ...) |
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| - | [[Image:1ya5.gif|left|200px]]<br /> | + | [[Image:1ya5.gif|left|200px]]<br /><applet load="1ya5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ya5" size=" | + | |
caption="1ya5, resolution 2.445Å" /> | caption="1ya5, resolution 2.445Å" /> | ||
'''Crystal structure of the titin domains z1z2 in complex with telethonin'''<br /> | '''Crystal structure of the titin domains z1z2 in complex with telethonin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Z-disk of striated and cardiac muscle sarcomeres is one of the most | + | The Z-disk of striated and cardiac muscle sarcomeres is one of the most densely packed cellular structures in eukaryotic cells. It provides the architectural framework for assembling and anchoring the largest known muscle filament systems by an extensive network of protein-protein interactions, requiring an extraordinary level of mechanical stability. Here we show, using X-ray crystallography, how the amino terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the Z-disk ligand telethonin. The pseudosymmetric structure of telethonin mediates a unique palindromic arrangement of two titin filaments, a type of molecular assembly previously found only in protein-DNA complexes. We have confirmed its unique architecture in vivo by protein complementation assays, and in vitro by experiments using fluorescence resonance energy transfer. The model proposed may provide a molecular paradigm of how major sarcomeric filaments are crosslinked, anchored and aligned within complex cytoskeletal networks. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YA5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YA5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YA5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: telethonin; t-cap; ig-like domains; z1; z2; titin]] | [[Category: telethonin; t-cap; ig-like domains; z1; z2; titin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:14 2008'' |
Revision as of 14:03, 21 February 2008
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Crystal structure of the titin domains z1z2 in complex with telethonin
Contents |
Overview
The Z-disk of striated and cardiac muscle sarcomeres is one of the most densely packed cellular structures in eukaryotic cells. It provides the architectural framework for assembling and anchoring the largest known muscle filament systems by an extensive network of protein-protein interactions, requiring an extraordinary level of mechanical stability. Here we show, using X-ray crystallography, how the amino terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the Z-disk ligand telethonin. The pseudosymmetric structure of telethonin mediates a unique palindromic arrangement of two titin filaments, a type of molecular assembly previously found only in protein-DNA complexes. We have confirmed its unique architecture in vivo by protein complementation assays, and in vitro by experiments using fluorescence resonance energy transfer. The model proposed may provide a molecular paradigm of how major sarcomeric filaments are crosslinked, anchored and aligned within complex cytoskeletal networks.
Disease
Known diseases associated with this structure: Cardiomyopathy, dilated, 1N OMIM:[604488], Muscular dystrophy, limb-girdle, type 2G OMIM:[604488]
About this Structure
1YA5 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk., Zou P, Pinotsis N, Lange S, Song YH, Popov A, Mavridis I, Mayans OM, Gautel M, Wilmanns M, Nature. 2006 Jan 12;439(7073):229-33. PMID:16407954
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