1tiu
From Proteopedia
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- | [[Image:1tiu.jpg|left|200px]] | + | [[Image:1tiu.jpg|left|200px]] |
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- | '''TITIN, IG REPEAT 27, NMR, 24 STRUCTURES''' | + | {{Structure |
+ | |PDB= 1tiu |SIZE=350|CAPTION= <scene name='initialview01'>1tiu</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= TITIN GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''TITIN, IG REPEAT 27, NMR, 24 STRUCTURES''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1TIU is a [ | + | 1TIU is a [[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=1TIU OCA]. |
==Reference== | ==Reference== | ||
- | Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity., Improta S, Politou AS, Pastore A, Structure. 1996 Mar 15;4(3):323-37. PMID:[http:// | + | Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity., Improta S, Politou AS, Pastore A, Structure. 1996 Mar 15;4(3):323-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8805538 8805538] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: muscle protein]] | [[Category: muscle protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:19:00 2008'' |
Revision as of 12:19, 20 March 2008
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Gene: | TITIN GENE (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
TITIN, IG REPEAT 27, NMR, 24 STRUCTURES
Overview
BACKGROUND. The giant muscle protein titin forms a filament which spans half of the sarcomere and performs, along its length, quite diverse functions. The region of titin located in the sarcomere I-band is believed to play a major role in extensibility and passive elasticity of muscle. In the I-band, the titin sequence consists mostly of repetitive motifs of tandem immunoglobulin-like (Ig) modules intercalated by a potentially non-globular region. The highly repetitive titin architecture suggests that the molecular basis of its mechanical properties be approached through the characterization of the isolated components of the I-band and their interfaces. In the present paper, we report on the structure determination in solution of a representative Ig module from the I-band (I27) as solved by NMR techniques. RESULTS. The structure of I27 consists of a beta sandwich formed by two four-stranded sheets (named ABED and A'GFC). This fold belongs to the intermediate frame (I frame) of the immunoglobulin superfamily. Comparison of I27 with another titin module from the region located in the M-line (M5) shows that two loops (between the B and C and the F and G strands) are shorter in I27, conferring a less elongated appearance to this structure. Such a feature is specific to the Ig domains in the I-band and might therefore be related to the functions of the protein in this region. The structure of tandem Ig domains as modeled from I27 suggests the presence of hinge regions connecting contiguous modules. CONCLUSIONS. We suggest that titin Ig domains in the I-band function as extensible components of muscle elasticity by stretching the hinge regions.
About this Structure
1TIU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity., Improta S, Politou AS, Pastore A, Structure. 1996 Mar 15;4(3):323-37. PMID:8805538
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