1dfv: Difference between revisions
New page: left|200px<br /> <applet load="1dfv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfv, resolution 2.60Å" /> '''CRYSTAL STRUCTURE O... |
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[[Image:1dfv.gif|left|200px]]<br /> | [[Image:1dfv.gif|left|200px]]<br /><applet load="1dfv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1dfv, resolution 2.60Å" /> | caption="1dfv, resolution 2.60Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN MONOMER'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN MONOMER'''<br /> | ||
==Overview== | ==Overview== | ||
Neutrophil gelatinase associated lipocalin (NGAL), a constituent of | Neutrophil gelatinase associated lipocalin (NGAL), a constituent of neutrophil granules, is a member of the lipocalin family of binding proteins. NGAL can also be highly induced in epithelial cells in both inflammatory and neoplastic colorectal disease. NGAL is proposed to mediate inflammatory responses by sequestering neutrophil chemoattractants, particularly N-formylated tripeptides and possibly leukotriene B(4) and platelet activating factor. The crystal structures of NGAL display a typical lipocalin fold, albeit with an unusually large and atypically polar binding site, or calyx. The fold of NGAL is most similar to the epididymal retinoic acid-binding protein, another lipocalin, though the overall architecture of the calyces are very different. The crystal structures also reveal either sulfate ions or an adventitiously copurified fatty acid bound in the binding site. Neither ligand is displaced by added N-formylated tripeptides. The size, shape, and character of the NGAL calyx, as well as the low relative affinity for N-formylated tripeptides, suggest that neither the copurified fatty acid nor any of the proposed ligands are likely to be the preferred ligand of this protein. Comparisons between the crystal structures and the recently reported solution structure of NGAL reveal significant differences, in terms of both the details of the structure and the overall flexibility of the fold. | ||
==About this Structure== | ==About this Structure== | ||
1DFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NDG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1DFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Armen, R | [[Category: Armen, R S.]] | ||
[[Category: Borregaard, N.]] | [[Category: Borregaard, N.]] | ||
[[Category: Bratt, T.]] | [[Category: Bratt, T.]] | ||
[[Category: Goetz, D | [[Category: Goetz, D H.]] | ||
[[Category: Strong, R | [[Category: Strong, R K.]] | ||
[[Category: Willie, S | [[Category: Willie, S T.]] | ||
[[Category: NDG]] | [[Category: NDG]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 26: | Line 25: | ||
[[Category: ngal]] | [[Category: ngal]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:15 2008'' | ||
Revision as of 13:16, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN MONOMER
OverviewOverview
Neutrophil gelatinase associated lipocalin (NGAL), a constituent of neutrophil granules, is a member of the lipocalin family of binding proteins. NGAL can also be highly induced in epithelial cells in both inflammatory and neoplastic colorectal disease. NGAL is proposed to mediate inflammatory responses by sequestering neutrophil chemoattractants, particularly N-formylated tripeptides and possibly leukotriene B(4) and platelet activating factor. The crystal structures of NGAL display a typical lipocalin fold, albeit with an unusually large and atypically polar binding site, or calyx. The fold of NGAL is most similar to the epididymal retinoic acid-binding protein, another lipocalin, though the overall architecture of the calyces are very different. The crystal structures also reveal either sulfate ions or an adventitiously copurified fatty acid bound in the binding site. Neither ligand is displaced by added N-formylated tripeptides. The size, shape, and character of the NGAL calyx, as well as the low relative affinity for N-formylated tripeptides, suggest that neither the copurified fatty acid nor any of the proposed ligands are likely to be the preferred ligand of this protein. Comparisons between the crystal structures and the recently reported solution structure of NGAL reveal significant differences, in terms of both the details of the structure and the overall flexibility of the fold.
About this StructureAbout this Structure
1DFV is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin., Goetz DH, Willie ST, Armen RS, Bratt T, Borregaard N, Strong RK, Biochemistry. 2000 Feb 29;39(8):1935-41. PMID:10684642
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