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Solution structure of a naturally-occurring zinc-peptide complex demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM domain is an independent folding unit
Karolinska Institutet.ORCID iD: 0000-0002-3049-967X
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1996 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 35, no 39, 12723-12732 p.Article in journal (Refereed) PublishedText
Abstract [en]

The three-dimensional solution structure of the 1:1 complex between the synthetic peptide ZF-1 and zinc was determined by H-1 NMR spectroscopy. The peptide, initially isolated from pig intestines, is identical in sequence to the 30 N-terminal amino acid residues of the human protein Lasp-1 belonging to the LIM domain protein family. The final set of 20 energy-refined NMR conformers has an average rmsd relative to the mean structure of 0.55 Angstrom for the backbone atoms of residues 3-30, Calculations without zinc atom constraints unambiguously identified Cys 5, Cys 8, His 26, and Cys 29 as the zinc-coordinating residues. LIM domains consist of two sequential zinc-binding modules and the NMR structure of the ZF-1(-)zinc complex is the first example of a structure of an isolated module. Comparison with the known structures of the N-terminal zinc-binding modules of both the second LIM domain of chicken CRP and rat GRIP with which ZF-1 shares 50% and 43% sequence identity, respectively, supports the notion that the zinc-binding modules of the LIM domain have a conserved structural motif and identifies local regions of structural diversity. The similarities include conserved zinc-coordinating residues, a rubredoxin knuckle involving Cys 5 and Cys 8, and the coordination of the zinc ion by histidine N-delta in contrast to the more usual coordination by N-epsilon observed for other zinc-finger domains, The present structure determination of the ZF-1(-)zinc complex establishes the N-terminal half of a LIM domain as an independent folding unit. The structural similarities of N- and C-terminal zinc-binding modules of the LIM domains, despite limited sequence identity, lead to the proposal of a single zinc-binding motif in LIM domains. The coordinates are available from the Brookhaven protein data bank, entry 1ZFO.

Place, publisher, year, edition, pages
1996. Vol. 35, no 39, 12723-12732 p.
Keyword [en]
cysteine-rich protein, differentiation, family, finger motif, gene, homeodomain, identification, nmr, nuclear-magnetic-resonance, spectroscopy
National Category
Structural Biology
URN: urn:nbn:se:sh:diva-29014DOI: 10.1021/bi961149jISI: A1996VK59400010ScopusID: 2-s2.0-0029816885OAI: diva2:892168

Times Cited: 23 Article English Cited References Count: 60 Vk594

Available from: 2016-01-08 Created: 2016-01-07 Last updated: 2016-01-11Bibliographically approved

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Berndt, Kurt D
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