2ck2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ck2.gif|left|200px]]<br /><applet load="2ck2" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2ck2.gif|left|200px]]
-
caption="2ck2, resolution 2.0&Aring;" />
+
 
-
'''STRUCTURE OF CORE-SWAPPED MUTANT OF FIBRONECTIN'''<br />
+
{{Structure
 +
|PDB= 2ck2 |SIZE=350|CAPTION= <scene name='initialview01'>2ck2</scene>, resolution 2.0&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Ace+Binding+Site+For+Chain+A'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''STRUCTURE OF CORE-SWAPPED MUTANT OF FIBRONECTIN'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
2CK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ace+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CK2 OCA].
+
2CK2 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=2CK2 OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17535921 17535921]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/17535921 17535921]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 35: Line 44:
[[Category: sulfation]]
[[Category: sulfation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:28 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:23 2008''

Revision as of 14:16, 20 March 2008

Image:2ck2.gif


PDB ID 2ck2

Drag the structure with the mouse to rotate
, resolution 2.0Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF CORE-SWAPPED MUTANT OF FIBRONECTIN


Contents

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.

Disease

Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]

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 Thu Mar 20 16:16:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ck2"
Personal tools