The solution structure of kringle 4. NMR studies on native and several chemically modified kringle 4 species of human plasminogen

M. Trexler, L. Bányai, L. Patthy, N. D. Pluck, R. J P Williams

Research output: Contribution to journalArticle

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Abstract

Kringle 4 of human plasminogen has been studied by NMR spectroscopy to define the solution structure of the kringle-fold and to characterize the ω-aminocarboxylic acid binding site. Aromatic and aliphatic resonances of the NMR spectrum have been identified with the aid of spin-decoupling and NOE procedures as well as pH-titration and metal ion probe studies. Comparison of the NMR spectrum of kringle 4 with the spectra of various kringle 4 species chemically modified at defined positions permitted the assignment of several resonances to specific residues in the kringle 4 sequence. The NOE studies revealed that Leu45 is in close proximity of the sequentially distant Trp25/Trp61 residue pair, thus delineating a definite structural feature of the kringle-fold. The binding of 6-aminohexanoic acid to kringle 4 was shown to cause shifts in the resonances of several aromatic residues, including those of Trp71, suggesting that several aromatic residues may be lining the ω-aminocarboxylic acid binding site. The binding of the ligand is competitive with the binding of lanthanide ions which reveal much detail of this site.

Original languageEnglish
Pages (from-to)311-318
Number of pages8
JournalFEBS Letters
Volume154
Issue number2
DOIs
Publication statusPublished - Apr 18 1983

Fingerprint

Kringles
Plasminogen
Nuclear magnetic resonance
Binding Sites
Aminocaproic Acid
Lanthanoid Series Elements
Acids
Titration
Linings
Nuclear magnetic resonance spectroscopy
Metal ions
Ions
Ligands
Competitive Binding
Magnetic Resonance Spectroscopy
Metals

Keywords

  • Human plasminogen
  • Kringle 4
  • NMR spectroscopy

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The solution structure of kringle 4. NMR studies on native and several chemically modified kringle 4 species of human plasminogen. / Trexler, M.; Bányai, L.; Patthy, L.; Pluck, N. D.; Williams, R. J P.

In: FEBS Letters, Vol. 154, No. 2, 18.04.1983, p. 311-318.

Research output: Contribution to journalArticle

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