1JFN

SOLUTION STRUCTURE OF HUMAN APOLIPOPROTEIN(A) KRINGLE IV TYPE 6

Summary for 1JFN

• Entry DOI: 10.2210/pdb1jfn/pdb
• NMR Information: BMRB: 5075
• Descriptor: APOLIPOPROTEIN A, KIV-T6 (1 entity in total)
• Functional Keywords: kringle domain, protein-protein recognition, lp(a), lipid transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 13588.77

Authors

Maderegger, B.,Bermel, W.,Hrzenjak, A.,Kostner, G.M.,Sterk, H. (deposition date: 2001-06-21, release date: 2002-06-28, Last modification date: 2024-11-06)

Primary citation

Maderegger, B.,Bermel, W.,Hrzenjak, A.,Kostner, G.M.,Sterk, H.
Solution structure of human apolipoprotein(a) kringle IV type 6.
Biochemistry, 41:660-668, 2002

PubMed 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.

PubMed: 11781107
DOI: 10.1021/bi011430k

Experimental method

SOLUTION NMR