1tmz: Difference between revisions

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[[Image:1tmz.gif|left|200px]]
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[[Image:1tmz.png|left|200px]]


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{{STRUCTURE_1tmz|  PDB=1tmz  |  SCENE=  }}  
{{STRUCTURE_1tmz|  PDB=1tmz  |  SCENE=  }}  


'''TMZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF ALPHA TROPOMYOSIN, NMR, 15 STRUCTURES'''
===TMZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF ALPHA TROPOMYOSIN, NMR, 15 STRUCTURES===




==Overview==
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Tropomyosins (TMs) are highly conserved, coiled-coil, actin binding regulatory proteins found in most eukaryotic cells. The amino-terminal domain of 284-residue TMs is among the most conserved and functionally important regions. The first nine residues are proposed to bind to the carboxyl-terminal nine residues to form the "overlap" region between successive TMs, which bind along the actin filament. Here, the structure of the N-terminus of muscle alpha-TM, in a chimeric peptide, TMZip, has been solved using circular dichroism (CD) and two-dimensional proton nuclear magnetic resonance (2D 1H NMR) spectroscopy. Residues 1-14 of TMZip are the first 14 N-terminal residues of rabbit striated alpha-TM, and residues 15-32 of TMZip are the last 18 C-terminal residues of the yeast GCN4 transcription factor. CD measurements show that TMZip forms a two-stranded coiled-coil alpha-helix with an enthalpy of folding of -34 +/- 2 kcal/mol. In 2D1H NMR studies at 15 degrees C, pH 6.4, the peptide exhibits 123 sequential and medium range intrachain NOE cross peaks per chain, characteristic of alpha-helices extending from residue 1 to residue 29, together with 85 long-range NOE cross peaks arising from interchain interactions. The three-dimensional structure of TMZip has been determined using these data plus an additional 509 intrachain constraints per chain. The coiled-coil domain extends to the N-terminus. Amide hydrogen exchange studies, however, suggest that the TM region is less stable than the GCN4 region. The work reported here is the first atomic-resolution structure of any region of TM and it allows insight into the mechanism of the function of the highly conserved N-terminal domain.
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{{ABSTRACT_PUBMED_9601044}}


==About this Structure==
==About this Structure==
1TMZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMZ OCA].  
1TMZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMZ OCA].  


==Reference==
==Reference==
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[[Category: Thin-filament-regulation]]
[[Category: Thin-filament-regulation]]
[[Category: Tropomyosin]]
[[Category: Tropomyosin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:01:05 2008''

Revision as of 21:01, 27 July 2008

File:1tmz.png

Template:STRUCTURE 1tmz

TMZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF ALPHA TROPOMYOSIN, NMR, 15 STRUCTURES

Template:ABSTRACT PUBMED 9601044

About this Structure

1TMZ is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

Reference

The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: nuclear magnetic resonance structure and circular dichroism studies., Greenfield NJ, Montelione GT, Farid RS, Hitchcock-DeGregori SE, Biochemistry. 1998 May 26;37(21):7834-43. PMID:9601044

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