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| - | [[Image:2ntd.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2ntd.png|left|200px]] |
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| | {{STRUCTURE_2ntd| PDB=2ntd | SCENE= }} | | {{STRUCTURE_2ntd| PDB=2ntd | SCENE= }} |
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| - | '''Human fibroblast growth factor-1 (140 amino acid form) with Cys117Val/Pro134Cys mutations'''
| + | ===Human fibroblast growth factor-1 (140 amino acid form) with Cys117Val/Pro134Cys mutations=== |
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| - | ==Overview==
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| - | The beta-trefoil protein human fibroblast growth factor-1 (FGF-1) is made up of a six-stranded antiparallel beta-barrel closed off on one end by three beta-hairpins, thus exhibiting a 3-fold axis of structural symmetry. The N and C terminus beta-strands hydrogen bond to each other and their interaction is postulated from both NMR and X-ray structure data to be important in folding and stability. Specific mutations within the adjacent N and C terminus beta-strands of FGF-1 are shown to provide a substantial increase in stability. This increase is largely correlated with an increased folding rate constant, and with a smaller but significant decrease in the unfolding rate constant. A series of stabilizing mutations are subsequently combined and result in a doubling of the DeltaG value of unfolding. When taken in the context of previous studies of stabilizing mutations, the results indicate that although FGF-1 is known for generally poor thermal stability, the beta-trefoil architecture appears capable of substantial thermal stability. Targeting stabilizing mutations within the N and C terminus beta-strand interactions of a beta-barrel architecture may be a generally useful approach to increase protein stability. Such stabilized mutations of FGF-1 are shown to exhibit significant increases in effective mitogenic potency, and may prove useful as "second generation" forms of FGF-1 for application in angiogenic therapy. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17570396}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17570396 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17570396}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Dubey, V K.]] | | [[Category: Dubey, V K.]] |
| | [[Category: Beta-trefoil]] | | [[Category: Beta-trefoil]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:53:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:39:09 2008'' |
Revision as of 09:39, 29 July 2008
Template:STRUCTURE 2ntd
Human fibroblast growth factor-1 (140 amino acid form) with Cys117Val/Pro134Cys mutations
Template:ABSTRACT PUBMED 17570396
About this Structure
2NTD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Spackling the crack: stabilizing human fibroblast growth factor-1 by targeting the N and C terminus beta-strand interactions., Dubey VK, Lee J, Somasundaram T, Blaber S, Blaber M, J Mol Biol. 2007 Aug 3;371(1):256-68. Epub 2007 May 31. PMID:17570396
Page seeded by OCA on Tue Jul 29 12:39:09 2008
