From Proteopedia
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| - | [[Image:1uuc.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1uuc| PDB=1uuc | SCENE= }} | | {{STRUCTURE_1uuc| PDB=1uuc | SCENE= }} |
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| - | '''SOLUTION STRUCTURE OF A CHIMERIC LEKTI-DOMAIN'''
| + | ===SOLUTION STRUCTURE OF A CHIMERIC LEKTI-DOMAIN=== |
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| - | ==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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15366933}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15366933 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15366933}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1UUC 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=1UUC OCA]. | + | 1UUC 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=1UUC OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Protease]] | | [[Category: Protease]] |
| | [[Category: Serine proteinase inhibitor]] | | [[Category: Serine proteinase inhibitor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:42:14 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:01:23 2008'' |
Revision as of 12:01, 29 July 2008
Template:STRUCTURE 1uuc
SOLUTION STRUCTURE OF A CHIMERIC LEKTI-DOMAIN
Template:ABSTRACT PUBMED 15366933
About this Structure
1UUC 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
Page seeded by OCA on Tue Jul 29 15:01:23 2008
