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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'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10339412}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10339412 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10339412}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 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]. | + | 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]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Mmp-9 component]] | | [[Category: Mmp-9 component]] |
| | [[Category: Transport protein]] | | [[Category: Transport protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:30:23 2008'' | + | |
| | + | ''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
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
