Medizinische Universität Graz - Research portal
Selected Publication:
Maderegger, B; Bermel, W; Hrzenjak, A; Kostner, GM; Sterk, H.
Solution structure of human apolipoprotein(a) kringle IV type 6.
Biochemistry. 2002; 41(2):660-668
Doi: 10.1021%2Fbi011430k
Web of Science
PubMed
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- Co-authors Med Uni Graz
- Hrzenjak Andelko
- Kostner Gerhard
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- Abstract:
- The structure of apo(a) KIVT6 was investigated by two- and three-dimensional homo- and heteronuclear NMR spectroscopy. The solution structure of apo(a) KIVT6 contains only a small amount of regular secondary structure elements, comprising a short piece of antiparallel beta-sheet formed by residues Trp62-Tyr64 and Trp72-Tyr74, a short piece of parallel beta-sheet formed by the residues Cys1-Tyr2 and Thr78-Gln79, and a small 3(10)-helix within residues Thr38-Tyr40. The backbone as well as the side chains are arranged in a way similar to those of apo(a) KIVT7, apo(a) KIVT10, and plasminogen K4. We determined additionally the K(d) value of 0.31 +/- 0.04 mM for the binding of epsilon-aminocaproic acid (EACA) to apo(a) KIVT6 and mapped the binding region on apo(a) KIVT6 by means of chemical shift perturbation. This lysine binding activity, which was reported to occur within apo(a) KIVT5-8, is functionally different from the lysine binding activity found for apo(a) KIVT10.
- Find related publications in this database (using NLM MeSH Indexing)
- Apolipoproteins - chemistry
- Apoprotein(a) - chemistry
- Binding Sites - chemistry
- Circular Dichroism - chemistry
- Crystallography, X-Ray - chemistry
- Cysteine - chemistry
- Escherichia coli - metabolism
- Humans - metabolism
- Kinetics - metabolism
- Kringles - metabolism
- Lipoprotein(a) - chemistry
- Magnetic Resonance Spectroscopy - chemistry
- Mass Spectrometry - chemistry
- Models, Molecular - chemistry
- Protein Binding - chemistry
- Protein Conformation - chemistry
- Protein Structure, Secondary - chemistry
- Protein Structure, Tertiary - chemistry
- Recombinant Proteins - chemistry