1uvf: Difference between revisions

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[[Image:1uvf.gif|left|200px]]
{{Seed}}
[[Image:1uvf.png|left|200px]]


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{{STRUCTURE_1uvf|  PDB=1uvf  |  SCENE=  }}  
{{STRUCTURE_1uvf|  PDB=1uvf  |  SCENE=  }}  


'''SOLUTION STRUCTURE OF THE STRUCTURED PART OF THE 15TH DOMAIN OF LEKTI'''
===SOLUTION STRUCTURE OF THE STRUCTURED PART OF THE 15TH DOMAIN OF LEKTI===




==Overview==
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The conversion of an alpha-helical to a beta-strand conformation and the presence of chameleon sequences are fascinating from the perspective that such structural features are implicated in the induction of amyloid-related fatal diseases. In this study, we have determined the solution structure of a chimeric domain (Dom1PI) from the multidomain Kazal-type serine proteinase inhibitor LEKTI using multidimensional NMR spectroscopy. This chimeric protein was constructed to investigate the reasons for differences in the folds of the homologous LEKTI domains 1 and 6 [Lauber, T., et al. (2003) J. Mol. Biol. 328, 205-219]. In Dom1PI, two adjacent phenylalanine residues (F28 and F29) of domain 1 were substituted with proline and isoleucine, respectively, as found in the corresponding P4' and P5' positions of domain 6. The three-dimensional structure of Dom1PI is significantly different from the structure of domain 1 and closely resembles the structure of domain 6, despite the sequence being identical to that of domain 1 except for the two substituted phenylalanine residues and being only 31% identical to the sequence of domain 6. The mutation converted a short 3(10)-helix into an extended loop conformation and parts of the long COOH-terminal alpha-helix of domain 1 into a beta-hairpin structure. The latter conformational change occurs in a sequence stretch distinct from the region containing the substituted residues. Therefore, this switch from an alpha-helical structure to a beta-hairpin structure indicates a chameleon sequence of seven residues. We conclude that the secondary structure of Dom1PI is determined not only by the local protein sequence but also by nonlocal interactions.
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{{ABSTRACT_PUBMED_15366933}}


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


==Reference==
==Reference==
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[[Category: Serine proteinase inhibitor]]
[[Category: Serine proteinase inhibitor]]
[[Category: Trypsin inhibitor]]
[[Category: Trypsin inhibitor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:44:20 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:38:06 2008''

Revision as of 15:38, 27 July 2008

File:1uvf.png

Template:STRUCTURE 1uvf

SOLUTION STRUCTURE OF THE STRUCTURED PART OF THE 15TH DOMAIN OF LEKTI

Template:ABSTRACT PUBMED 15366933

About this Structure

1UVF is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

The solution structure of a chimeric LEKTI domain reveals a chameleon sequence., Tidow H, Lauber T, Vitzithum K, Sommerhoff CP, Rosch P, Marx UC, Biochemistry. 2004 Sep 7;43(35):11238-47. PMID:15366933

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