The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin

Coles M, Diercks T, Muehlenweg B, Bartsch S, Zolzer V, Tschesche H, Kessler H (1999)
JOURNAL OF MOLECULAR BIOLOGY 289(1): 139-157.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract
Human neutrophil gelatinase-associated lipocalin (HNGAL) is a member of the lipocalin family of extracellular proteins that function as transporters of small, hydrophobic molecules. HNGAL, a component of human blood granulocytes, binds bacterially derived formyl peptides that act as chemotactic agents and induce leukocyte granule discharge. HNGAL also forms a complex with the proenzyme form of matrix metalloproteinase-9 (pro-MMP-9, or progelatinase B) via an intermolecular disulphide bridge. This association allows the subsequent formation of ternary and quaternary metalloproteinase/inhibitor complexes that vary greatly in their metalloproteinase activities. The structure and dynamics of apo-HNGAL have been determined by NMR spectroscopy. Simulated annealing calculations yielded a set of 20 convergent structures with an average backbone RMSD from mean coordinate positions of 0.79(+/-0.13) Angstrom over secondary structure elements. The overall rotational correlation time (13.3 ns) derived from N-15 relaxation data is consistent with a monomeric protein of the size of HNGAL (179 residues) under the experimental conditions (1.4 mM protein, pH 6.0, 24.5 degrees C). The structure features an eight stranded antiparallel beta-barrel, typical of the lipocalin family. One end of the barrel is open, providing access to the binding site within the barrel cavity, while the other is closed by a short 3(10)-helix. The free cysteine residue required for association with pro-MMP-9 lies in an inter-strand loop at the closed end of the barrel. The structure provides a detailed model of the ligand-binding site and has led to the proposal of a site for pro-MMP-9 association. Dynamic data correlate well with structural features, which has allowed us to investigate a mechanism by which a cell-surface receptor might distinguish between apo and holo-HNGAL through conformational changes at the open end of the barrel. (C) 1999 Academic Press.
Publishing Year
ISSN
PUB-ID

Cite this

Coles M, Diercks T, Muehlenweg B, et al. The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin. JOURNAL OF MOLECULAR BIOLOGY. 1999;289(1):139-157.
Coles, M., Diercks, T., Muehlenweg, B., Bartsch, S., Zolzer, V., Tschesche, H., & Kessler, H. (1999). The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin. JOURNAL OF MOLECULAR BIOLOGY, 289(1), 139-157.
Coles, M., Diercks, T., Muehlenweg, B., Bartsch, S., Zolzer, V., Tschesche, H., and Kessler, H. (1999). The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin. JOURNAL OF MOLECULAR BIOLOGY 289, 139-157.
Coles, M., et al., 1999. The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin. JOURNAL OF MOLECULAR BIOLOGY, 289(1), p 139-157.
M. Coles, et al., “The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin”, JOURNAL OF MOLECULAR BIOLOGY, vol. 289, 1999, pp. 139-157.
Coles, M., Diercks, T., Muehlenweg, B., Bartsch, S., Zolzer, V., Tschesche, H., Kessler, H.: The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin. JOURNAL OF MOLECULAR BIOLOGY. 289, 139-157 (1999).
Coles, M, Diercks, T, Muehlenweg, B, Bartsch, S, Zolzer, V, Tschesche, Harald, and Kessler, H. “The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin”. JOURNAL OF MOLECULAR BIOLOGY 289.1 (1999): 139-157.
This data publication is cited in the following publications:
This publication cites the following data publications:

33 Citations in Europe PMC

Data provided by Europe PubMed Central.

Evaluation of Early Markers of Nephropathy in Patients with Type 2 Diabetes Mellitus.
De Muro P, Lepedda AJ, Nieddu G, Idini M, Tram Nguyen HQ, Lobina O, Fresu P, Formato M., Biochem Res Int 2016(), 2016
PMID: 26904288
Assessment of kidney function in diabetic patients. Is there a role for new biomarkers NGAL, cystatin C and KIM-1?
Matys U, Bachorzewska-Gajewska H, Malyszko J, Dobrzycki S., Adv Med Sci 58(2), 2013
PMID: 24384771
Supporting immunoassay design with biophysical tools.
Ruan Q, Saldana SC, Grenier FC, Tetin SY., Anal. Biochem. 437(1), 2013
PMID: 23453975
A new model for mapping the peptide backbone: predicting proton chemical shifts in proteins.
Barneto JL, Avalos M, Babiano R, Cintas P, Jimenez JL, Palacios JC., Org. Biomol. Chem. 8(4), 2010
PMID: 20135044
Model-free analysis for large proteins at high magnetic field strengths.
Chang SL, Hinck AP, Ishima R., J. Biomol. NMR 38(4), 2007
PMID: 17593525
Methyl dynamics in crystalline amino acids: MD and NMR.
Chatfield DC, Augsten A, D'Cunha C, Wong SE., J Comput Chem 24(9), 2003
PMID: 12759905
NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.
Alexandrescu AT, Lamour FP, Jaravine VA., J. Mol. Biol. 295(2), 2000
PMID: 10623523

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 10339412
PubMed | Europe PMC

Search this title in

Google Scholar