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| - | [[Image:2f21.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2f21.png|left|200px]] |
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| | {{STRUCTURE_2f21| PDB=2f21 | SCENE= }} | | {{STRUCTURE_2f21| PDB=2f21 | SCENE= }} |
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| - | '''human Pin1 Fip mutant'''
| + | ===human Pin1 Fip mutant=== |
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| - | ==Overview==
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| - | Protein folding barriers result from a combination of factors including unavoidable energetic frustration from nonnative interactions, natural variation and selection of the amino acid sequence for function, and/or selection pressure against aggregation. The rate-limiting step for human Pin1 WW domain folding is the formation of the loop 1 substructure. The native conformation of this six-residue loop positions side chains that are important for mediating protein-protein interactions through the binding of Pro-rich sequences. Replacement of the wild-type loop 1 primary structure by shorter sequences with a high propensity to fold into a type-I' beta-turn conformation or the statistically preferred type-I G1 bulge conformation accelerates WW domain folding by almost an order of magnitude and increases thermodynamic stability. However, loop engineering to optimize folding energetics has a significant downside: it effectively eliminates WW domain function according to ligand-binding studies. The energetic contribution of loop 1 to ligand binding appears to have evolved at the expense of fast folding and additional protein stability. Thus, the two-state barrier exhibited by the wild-type human Pin1 WW domain principally results from functional requirements, rather than from physical constraints inherent to even the most efficient loop formation process.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16807295}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16807295 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16807295}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Beta-sheet]] | | [[Category: Beta-sheet]] |
| | [[Category: Ww domain]] | | [[Category: Ww domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:22:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:42:05 2008'' |
Revision as of 14:42, 28 July 2008
Template:STRUCTURE 2f21
human Pin1 Fip mutant
Template:ABSTRACT PUBMED 16807295
About this Structure
2F21 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure-function-folding relationship in a WW domain., Jager M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW, Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10648-53. Epub 2006 Jun 28. PMID:16807295
Page seeded by OCA on Mon Jul 28 17:42:05 2008
