1tl2
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tl2 OCA], [http://www.ebi.ac.uk/pdbsum/1tl2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tl2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Iwanaga, S.]] | [[Category: Iwanaga, S.]] | ||
[[Category: Kawabata, S.]] | [[Category: Kawabata, S.]] | ||
- | [[Category: NDG]] | ||
[[Category: animal lectin]] | [[Category: animal lectin]] | ||
[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
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[[Category: n-acetylglucosamine]] | [[Category: n-acetylglucosamine]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:57:33 2008'' |
Revision as of 20:57, 30 March 2008
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, resolution 2.0Å | |||||||
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Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
TACHYLECTIN-2 FROM TACHYPLEUS TRIDENTATUS (JAPANESE HORSESHOE CRAB)
Overview
Tachylectin-2, isolated from large granules of the hemocytes of the Japanese horseshoe crab (Tachypleus tridentatus), is a 236 amino acid protein belonging to the lectins. It binds specifically to N-acetylglucosamine and N-acetylgalactosamine and is a part of the innate immunity host defense system of the horseshoe crab. The X-ray structure of tachylectin-2 was solved at 2.0 A resolution by the multiple isomorphous replacement method and this molecular model was employed to solve the X-ray structure of the complex with N-acetylglucosamine. Tachylectin-2 is the first protein displaying a five-bladed beta-propeller structure. Five four-stranded antiparallel beta-sheets of W-like topology are arranged around a central water-filled tunnel, with the water molecules arranged as a pentagonal dodecahedron. Tachylectin-2 exhibits five virtually identical binding sites, one in each beta-sheet. The binding sites are located between adjacent beta-sheets and are made by a large loop between the outermost strands of the beta-sheets and the connecting segment from the previous beta-sheet. The high number of five binding sites within the single polypeptide chain strongly suggests the recognition of carbohydrate surface structures of pathogens with a fairly high ligand density. Thus, tachylectin-2 employs strict specificity for certain N-acetyl sugars as well as the surface ligand density for self/non-self recognition.
About this Structure
1TL2 is a Single protein structure of sequence from Tachypleus tridentatus. Full crystallographic information is available from OCA.
Reference
Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus., Beisel HG, Kawabata S, Iwanaga S, Huber R, Bode W, EMBO J. 1999 May 4;18(9):2313-22. PMID:10228146
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