2ck2
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2ck2.gif|left|200px]] | [[Image:2ck2.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2ck2", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_2ck2| PDB=2ck2 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''STRUCTURE OF CORE-SWAPPED MUTANT OF FIBRONECTIN''' | '''STRUCTURE OF CORE-SWAPPED MUTANT OF FIBRONECTIN''' | ||
| Line 33: | Line 30: | ||
[[Category: Ohashi, T.]] | [[Category: Ohashi, T.]] | ||
[[Category: Randles, L G.]] | [[Category: Randles, L G.]] | ||
| - | [[Category: | + | [[Category: Acute phase]] |
| - | [[Category: | + | [[Category: Alternative splicing]] |
| - | [[Category: | + | [[Category: Cell adhesion]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Heparin-binding]] |
| - | [[Category: | + | [[Category: Phosphorylation]] |
| - | [[Category: | + | [[Category: Pyrrolidone carboxylic acid]] |
| - | [[Category: | + | [[Category: Signaling protein]] |
| - | [[Category: | + | [[Category: Sulfation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:20:05 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:20, 3 May 2008
STRUCTURE OF CORE-SWAPPED MUTANT OF FIBRONECTIN
Overview
The extracellular matrix proteins tenascin and fibronectin experience significant mechanical forces in vivo. Both contain a number of tandem repeating homologous fibronectin type III (fnIII) domains, and atomic force microscopy experiments have demonstrated that the mechanical strength of these domains can vary significantly. Previous work has shown that mutations in the core of an fnIII domain from human tenascin (TNfn3) reduce the unfolding force of that domain significantly: The composition of the core is apparently crucial to the mechanical stability of these proteins. Based on these results, we have used rational redesign to increase the mechanical stability of the 10th fnIII domain of human fibronectin, FNfn10, which is directly involved in integrin binding. The hydrophobic core of FNfn10 was replaced with that of the homologous, mechanically stronger TNfn3 domain. Despite the extensive substitution, FNoTNc retains both the three-dimensional structure and the cell adhesion activity of FNfn10. Atomic force microscopy experiments reveal that the unfolding forces of the engineered protein FNoTNc increase by approximately 20% to match those of TNfn3. Thus, we have specifically designed a protein with increased mechanical stability. Our results demonstrate that core engineering can be used to change the mechanical strength of proteins while retaining functional surface interactions.
About this Structure
2CK2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Designing an extracellular matrix protein with enhanced mechanical stability., Ng SP, Billings KS, Ohashi T, Allen MD, Best RB, Randles LG, Erickson HP, Clarke J, Proc Natl Acad Sci U S A. 2007 Jun 5;104(23):9633-7. Epub 2007 May 29. PMID:17535921 Page seeded by OCA on Sat May 3 22:20:05 2008
Categories: Homo sapiens | Single protein | Allen, M D. | Best, R B. | Billings, K S. | Clarke, J. | Erickson, H P. | Ng, S P. | Ohashi, T. | Randles, L G. | Acute phase | Alternative splicing | Cell adhesion | Glycoprotein | Heparin-binding | Phosphorylation | Pyrrolidone carboxylic acid | Signaling protein | Sulfation
