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1nay

From Proteopedia

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[[Image:1nay.gif|left|200px]]
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{{STRUCTURE_1nay| PDB=1nay | SCENE= }}
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'''GPP-Foldon:X-ray structure'''
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===GPP-Foldon:X-ray structure===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12623021 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12623021}}
==About this Structure==
==About this Structure==
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[[Category: Stetefeld, J.]]
[[Category: Stetefeld, J.]]
[[Category: Collagen assembly]]
[[Category: Collagen assembly]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:18:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:15:22 2008''

Revision as of 18:15, 27 July 2008

Image:1nay.png

Template:STRUCTURE 1nay

GPP-Foldon:X-ray structure

Template:ABSTRACT PUBMED 12623021

About this Structure

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

Page seeded by OCA on Sun Jul 27 21:15:22 2008

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