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1tl2
From Proteopedia
(New page: 200px<br /><applet load="1tl2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tl2, resolution 2.0Å" /> '''TACHYLECTIN-2 FROM TA...) |
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| - | [[Image:1tl2.jpg|left|200px]]<br /><applet load="1tl2" size=" | + | [[Image:1tl2.jpg|left|200px]]<br /><applet load="1tl2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tl2, resolution 2.0Å" /> | caption="1tl2, resolution 2.0Å" /> | ||
'''TACHYLECTIN-2 FROM TACHYPLEUS TRIDENTATUS (JAPANESE HORSESHOE CRAB)'''<br /> | '''TACHYLECTIN-2 FROM TACHYPLEUS TRIDENTATUS (JAPANESE HORSESHOE CRAB)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tachylectin-2, isolated from large granules of the hemocytes of the | + | 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== | ==About this Structure== | ||
| - | 1TL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus] with NDG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus] with <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TL2 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tachypleus tridentatus]] | [[Category: Tachypleus tridentatus]] | ||
| - | [[Category: Beisel, H | + | [[Category: Beisel, H G.]] |
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
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[[Category: n-acetylglucosamine]] | [[Category: n-acetylglucosamine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:47 2008'' |
Revision as of 13:14, 21 February 2008
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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 with as ligand. 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
Page seeded by OCA on Thu Feb 21 15:14:47 2008
