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1nay

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Image:1nay.gif

GPP-Foldon:X-ray structure

Overview

In a designed fusion protein the trimeric domain foldon from bacteriophage, T4 fibritin was connected to the C terminus of the collagen model peptide, (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the, three-stranded collagen triple helix. Crystal structure analysis at 2.6 A, resolution revealed conformational changes within the interface of both, domains compared with the structure of the isolated molecules. A striking, feature is an angle of 62.5 degrees between the symmetry axis of the, foldon trimer and the axis of the triple helix. The melting temperature of, (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is, higher than that of isolated (GlyProPro)(10,) which suggests an entropic, stabilization compensating for the destabilization at the interface.

About this Structure

1NAY is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon., Stetefeld J, Frank S, Jenny M, Schulthess T, Kammerer RA, Boudko S, Landwehr R, Okuyama K, Engel J, Structure. 2003 Mar;11(3):339-46. PMID:12623021

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