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1ngl

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{{STRUCTURE_1ngl| PDB=1ngl | SCENE= }}
{{STRUCTURE_1ngl| PDB=1ngl | SCENE= }}
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'''HUMAN NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN (HNGAL), REGULARISED AVERAGE NMR STRUCTURE'''
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===HUMAN NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN (HNGAL), REGULARISED AVERAGE NMR STRUCTURE===
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==Overview==
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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) A over secondary structure elements. The overall rotational correlation time (13.3 ns) derived from15N 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 310-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.
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{{ABSTRACT_PUBMED_10339412}}
==About this Structure==
==About this Structure==
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1NGL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NGL OCA].
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1NGL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NGL OCA].
==Reference==
==Reference==
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[[Category: Mmp-9 component]]
[[Category: Mmp-9 component]]
[[Category: Transport protein]]
[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:30:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:04:21 2008''

Revision as of 15:04, 27 July 2008

Image:1ngl.png

Template:STRUCTURE 1ngl

HUMAN NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN (HNGAL), REGULARISED AVERAGE NMR STRUCTURE

Template:ABSTRACT PUBMED 10339412

About this Structure

1NGL is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

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, J Mol Biol. 1999 May 28;289(1):139-57. PMID:10339412

Page seeded by OCA on Sun Jul 27 18:04:21 2008

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