NMR Solution Structure of a Chymotrypsin Inhibitor from the Taiwan Cobra Naja naja atra
| Autor: | Teppei Ikeya, Long-Sen Chang, Yi-Jan Lin, Peter Güntert |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Stereochemistry
Protein Conformation Naja Taiwan Pharmaceutical Science Antiparallel (biochemistry) Article Protein Structure Secondary Analytical Chemistry lcsh:QD241-441 NMR spectroscopy ddc:590 lcsh:Organic chemistry NACI ddc:570 Drug Discovery Animals Chymotrypsin Protease Inhibitors Elapidae Physical and Theoretical Chemistry Nuclear Magnetic Resonance Biomolecular snake venom chemistry.chemical_classification Binding Sites biology Organic Chemistry Nuclear magnetic resonance spectroscopy disulfide bond isomerization biology.organism_classification Protein tertiary structure Amino acid Protein Structure Tertiary chymotrypsin inhibitor chemistry Chemistry (miscellaneous) Snake venom Naja naja atra Molecular Medicine Cattle NMR structure determination Isomerization Two-dimensional nuclear magnetic resonance spectroscopy BPTI |
| Zdroj: | Molecules, Vol 18, Iss 8, Pp 8906-8918 (2013) Molecules Volume 18 Issue 8 Pages 8906-8918 |
| ISSN: | 1420-3049 |
| Popis: | The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin inhibitor. Here we present the solution structure of NACI. We determined the NMR structure of NACI with a root-mean-square deviation of 0.37 A for the backbone atoms and 0.73 A for the heavy atoms on the basis of 1,075 upper distance limits derived from NOE peaks measured in its NOESY spectra. To investigate the structural characteristics of NACI, we compared the three-dimensional structure of NACI with BPTI and BF9. The structure of the NACI protein comprises one 310-helix, one α-helix and one double-stranded antiparallel β-sheet, which is comparable with the secondary structures in BPTI and BF9. The RMSD value between the mean structures is 1.09 A between NACI and BPTI and 1.27 A between NACI and BF9. In addition to similar secondary and tertiary structure, NACI might possess similar types of protein conformational fluctuations as reported in BPTI, such as Cys14–Cys38 disulfide bond isomerization, based on line broadening of resonances from residues which are mainly confined to a region around the Cys14–Cys38 disulfide bond. |
| Databáze: | OpenAIRE |
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