1xki
From Proteopedia
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|PDB= 1xki |SIZE=350|CAPTION= <scene name='initialview01'>1xki</scene>, resolution 1.80Å | |PDB= 1xki |SIZE=350|CAPTION= <scene name='initialview01'>1xki</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= LCN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= LCN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xki OCA], [http://www.ebi.ac.uk/pdbsum/1xki PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xki RCSB]</span> | ||
}} | }} | ||
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[[Category: Redl, B.]] | [[Category: Redl, B.]] | ||
[[Category: Skerra, A.]] | [[Category: Skerra, A.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: ZN]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: ligand binding protein]] | [[Category: ligand binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:50:54 2008'' |
Revision as of 21:50, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | LCN1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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