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Solution structure and functional characterization of human plasminogen kringle 5.

Marcos D Battistel1, Alexander Grishaev, Seong Soo A An

  • 1Department of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, USA.

Biochemistry
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PubMed
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The kringle 5 domain of human plasminogen binds oleic acid and competes with AMCHA at the lysine binding site. This binding site exhibits structural flexibility, suggesting diverse biological roles for kringle domains.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Human plasminogen's kringle 5 (K5) domain plays a role in fibrinolysis.
  • Understanding ligand interactions with K5 is crucial for elucidating its biological functions.

Purpose of the Study:

  • To investigate the ligand binding properties of the human plasminogen K5 domain.
  • To characterize the binding of oleic acid (OA) and trans-4-(aminomethyl)cyclohexanecarboxylic acid (AMCHA) to K5.
  • To determine the structural basis of ligand binding to K5.

Main Methods:

  • Intrinsic tryptophan fluorescence spectroscopy to quantify ligand affinity.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to solve the solution structure of K5.
  • Hydrogen/Nitrogen-15 chemical shift perturbation mapping and in silico docking to localize binding sites.

Main Results:

  • OA binds to K5 with an association constant (K(a)) of approximately 2.08 x 10(4) mM(-1).
  • OA and AMCHA compete for binding to K5, with AMCHA having a K(a) of approximately 50 mM(-1).
  • AMCHA binds to the canonical lysine binding site (LBS) of K5, involving specific residues and exhibiting structural flexibility in the surrounding segment.
  • OA also perturbs the LBS and Tyr74, indicating overlapping binding interactions.

Conclusions:

  • The K5 domain binds OA at its LBS, a site also recognized by AMCHA.
  • The structural flexibility of the LBS region may be important for ligand binding.
  • The binding of OA expands the known ligand repertoire for K5 and suggests broader biological roles for kringle domains.