1tmr
From Proteopedia
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THE STRUCTURE OF A 19 RESIDUE FRAGMENT FROM THE C-LOOP OF THE FOURTH EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF THROMBOMODULIN
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Overview
The solution structure has been determined for a 19-residue peptide that, is fully folded at room temperature. The sequence of this peptide is based, on the C-loop, residues 371-389, of the fourth epidermal growth, factor-like domain of thrombomodulin, a protein that acts as a cofactor, for the thrombin activation of protein C. Despite its small size, the, peptide forms a compact structure with almost no repeating secondary, structure. The results indicate the structure is held together by, hydrophobic interactions, which in turn stabilize the two beta-turns in, the structure. The first beta-turn in the C-loop represents a conserved, motif that is found in the published structures of five other epidermal, growth factor-like proteins. The critical role of Phe376 in the, stabilization of the first beta-turn is consistent with mutagenesis data, with soluble thrombomodulin. The results also show that a small subdomain, of a larger protein can fold independently, and therefore it could act as, an initiation site for further folding.
Disease
Known diseases associated with this structure: Myocardial infarction, susceptibility to OMIM:[188040], Thrombophilia due to thrombomodulin defect OMIM:[188040]
About this Structure
1TMR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin., Adler M, Seto MH, Nitecki DE, Lin JH, Light DR, Morser J, J Biol Chem. 1995 Oct 6;270(40):23366-72. PMID:7559494
Page seeded by OCA on Fri Feb 15 16:57:48 2008
