1TMR

THE STRUCTURE OF A 19 RESIDUE FRAGMENT FROM THE C-LOOP OF THE FOURTH EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF THROMBOMODULIN

Summary for 1TMR

• Entry DOI: 10.2210/pdb1tmr/pdb
• Descriptor: THROMBOMODULIN PRECURSOR (1 entity in total)
• Functional Keywords: blood coagulation
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P07204
• Total number of polymer chains: 1
• Total formula weight: 2073.40

Authors

Adler, M.,Seto, M.,Nitecki, D.,Light, D.R.,Morser, J. (deposition date: 1994-05-20, release date: 1995-06-08, Last modification date: 2024-10-16)

Primary citation

Adler, M.,Seto, M.H.,Nitecki, D.E.,Lin, J.H.,Light, D.R.,Morser, J.
The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin.
J.Biol.Chem., 270:23366-23372, 1995

PubMed Abstract: 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.

PubMed: 7559494
DOI: 10.1074/jbc.270.40.23366

Experimental method

SOLUTION NMR