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1bpv
From Proteopedia
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[[Image:1bpv.gif|left|200px]] | [[Image:1bpv.gif|left|200px]] | ||
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'''TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES''' | '''TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES''' | ||
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[[Category: Nilges, M.]] | [[Category: Nilges, M.]] | ||
[[Category: Pastore, A.]] | [[Category: Pastore, A.]] | ||
| - | [[Category: | + | [[Category: Connectin]] |
| - | [[Category: | + | [[Category: Fibronectin type iii]] |
| - | [[Category: | + | [[Category: Titin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:48:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:48, 2 May 2008
TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES
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.
About this Structure
1BPV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains., Goll CM, Pastore A, Nilges M, Structure. 1998 Oct 15;6(10):1291-302. PMID:9782056 Page seeded by OCA on Fri May 2 11:48:31 2008
