1xki
From Proteopedia
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- | [[Image:1xki.gif|left|200px]] | + | [[Image:1xki.gif|left|200px]] |
- | + | ||
- | '''Crystal structure of human tear lipocalin/von Ebners gland protein''' | + | {{Structure |
+ | |PDB= 1xki |SIZE=350|CAPTION= <scene name='initialview01'>1xki</scene>, resolution 1.80Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= LCN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of human tear lipocalin/von Ebners gland protein''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1XKI is a [ | + | 1XKI 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=1XKI OCA]. |
==Reference== | ==Reference== | ||
- | The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands., Breustedt DA, Korndorfer IP, Redl B, Skerra A, J Biol Chem. 2005 Jan 7;280(1):484-93. Epub 2004 Oct 15. PMID:[http:// | + | The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands., Breustedt DA, Korndorfer IP, Redl B, Skerra A, J Biol Chem. 2005 Jan 7;280(1):484-93. Epub 2004 Oct 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15489503 15489503] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ligand binding protein]] | [[Category: ligand binding protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:10:59 2008'' |
Revision as of 13:10, 20 March 2008
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, resolution 1.80Å | |||||||
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Ligands: | and | ||||||
Gene: | LCN1 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of human tear lipocalin/von Ebners gland protein
Overview
In contrast with earlier assumptions, which classified human tear lipocalin (Tlc) as an outlier member of the lipocalin protein family, the 1.8-A resolution crystal structure of the recombinant apoprotein confirms the typical eight-stranded antiparallel beta-barrel architecture with an alpha-helix attached to it. The fold of Tlc most closely resembles the bovine dander allergen Bos d 2, a well characterized prototypic lipocalin, but also reveals similarity with beta-lactoglobulin. However, compared with other lipocalin structures Tlc exhibits an extremely wide ligand pocket, whose entrance is formed by four partially disordered loops. The cavity deeply extends into the beta-barrel structure, where it ends in two distinct lobes. This unusual structural feature explains the known promiscuity of Tlc for various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampin and even to microbial siderophores. Notably, earlier findings of biological activity as a thiol protease inhibitor have no correspondence in the three-dimensional structure of Tlc, rather it appears that its proteolytic fragments could be responsible for this phenomenon. Hence, the present structural analysis sheds new light on the ligand binding activity of this functionally obscure but abundant human lipocalin.
About this Structure
1XKI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands., Breustedt DA, Korndorfer IP, Redl B, Skerra A, J Biol Chem. 2005 Jan 7;280(1):484-93. Epub 2004 Oct 15. PMID:15489503
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