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| - | [[Image:2rfm.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2rfm| PDB=2rfm | SCENE= }} | | {{STRUCTURE_2rfm| PDB=2rfm | SCENE= }} |
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| - | '''Structure of a Thermophilic Ankyrin Repeat Protein'''
| + | ===Structure of a Thermophilic Ankyrin Repeat Protein=== |
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| - | ==Overview==
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| - | Repeat proteins are widespread in nature, with many of them functioning as binding molecules in protein-protein recognition. Their simple structural architecture is used in biotechnology for generating proteins with high affinities to target proteins. Recent folding studies of ankyrin repeat (AR) proteins revealed a new mechanism of protein folding. The formation of an intermediate state is rate limiting in the folding reaction, suggesting a scaffold function of this transient state for intrinsically less stable ARs. To investigate a possible common mechanism of AR folding, we studied the structure and folding of a new thermophilic AR protein (tANK) identified in the archaeon Thermoplasma volcanium. The x-ray structure of the evolutionary much older tANK revealed high homology to the human CDK inhibitor p19(INK4d), whose sequence was used for homology search. As for p19(INK4d), equilibrium and kinetic folding analyses classify tANK to the family of sequential three-state folding proteins, with an unusual fast equilibrium between native and intermediate state. Under equilibrium conditions, the intermediate can be populated to >90%, allowing characterization on a residue-by-residue level using NMR spectroscopy. These data clearly show that the three C-terminal ARs are natively folded in the intermediate state, whereas native cross-peaks for the rest of the molecule are missing. Therefore, the formation of a stable folding unit consisting of three ARs is the necessary rate-limiting step before AR 1 and 2 can assemble to form the native state.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18305166}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18305166 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18305166}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ankyrin repeat]] | | [[Category: Ankyrin repeat]] |
| | [[Category: Protein binding]] | | [[Category: Protein binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:49:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:57:52 2008'' |
Revision as of 11:58, 28 July 2008
Template:STRUCTURE 2rfm
Structure of a Thermophilic Ankyrin Repeat Protein
Template:ABSTRACT PUBMED 18305166
About this Structure
2RFM is a Single protein structure of sequence from Thermoplasma volcanium. Full crystallographic information is available from OCA.
Reference
Structural insights into an equilibrium folding intermediate of an archaeal ankyrin repeat protein., Low C, Weininger U, Neumann P, Klepsch M, Lilie H, Stubbs MT, Balbach J, Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3779-84. Epub 2008 Feb 27. PMID:18305166
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