2ck2

From Proteopedia

Revision as of 15:06, 30 October 2007

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, ... [(full description)]

About this Structure

2CK2 is a [Single protein] structure of sequence from [Homo sapiens] with ACE as [ligand]. Structure known Active Site: AC1. 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

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