1jc9

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(Difference between revisions)

Revision as of 00:11, 12 September 2015

TACHYLECTIN 5A FROM TACHYPLEUS TRIDENTATUS (JAPANESE HORSESHOE CRAB)

Structural highlights

1jc9 is a 1 chain structure with sequence from Tachypleus tridentatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1tl2, 1aoc
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TL5A_TACTR] Lectin involved in innate immunity. Agglutinates all types of human erythrocytes, Gram-positive and Gram-negative bacteria. Has a stronger agglutinating activity towards Gram-negative bacteria than towards Gram-positive bacteria. Specifically recognizes acetyl group-containing substances on agglutinated cells. The hemagglutinating activity was inhibited by EDTA, acetyl group-containing mono- and disaccharides, N-acetyl derivatives of amino acids, other acetyl group-containing substances, propionamide and benzamide. Enhances the antimicrobial activity of big defensin against Gram-positive bacteria but not against Gram-negative bacteria.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Because invertebrates lack an adaptive immune system, they had to evolve effective intrinsic defense strategies against a variety of microbial pathogens. This ancient form of host defense, the innate immunity, is present in all multicellular organisms including humans. The innate immune system of the Japanese horseshoe crab Tachypleus tridentatus, serving as a model organism, includes a hemolymph coagulation system, which participates both in defense against microbes and in hemostasis. Early work on the evolution of vertebrate fibrinogen suggested a common origin of the arthropod hemolymph coagulation and the vertebrate blood coagulation systems. However, this conjecture could not be verified by comparing the structures of coagulogen, the clotting protein of the horseshoe crab, and of mammalian fibrinogen. Here we report the crystal structure of tachylectin 5A (TL5A), a nonself-recognizing lectin from the hemolymph plasma of T. tridentatus. TL5A shares not only a common fold but also related functional sites with the gamma fragment of mammalian fibrinogen. Our observations provide the first structural evidence of a common ancestor for the innate immunity and the blood coagulation systems.

The 2.0-A crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems.,Kairies N, Beisel HG, Fuentes-Prior P, Tsuda R, Muta T, Iwanaga S, Bode W, Huber R, Kawabata S Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13519-24. Epub 2001 Nov 13. PMID:11707569^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gokudan S, Muta T, Tsuda R, Koori K, Kawahara T, Seki N, Mizunoe Y, Wai SN, Iwanaga S, Kawabata S. Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen. Proc Natl Acad Sci U S A. 1999 Aug 31;96(18):10086-91. PMID:10468566
↑ Kairies N, Beisel HG, Fuentes-Prior P, Tsuda R, Muta T, Iwanaga S, Bode W, Huber R, Kawabata S. The 2.0-A crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13519-24. Epub 2001 Nov 13. PMID:11707569 doi:http://dx.doi.org/10.1073/pnas.201523798

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jc9"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tl2|1tl2]], [[1aoc|1aoc]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1jc9 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc9 OCA], [http://pdbe.org/1jc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1jc9 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TL5A_TACTR TL5A_TACTR]] Lectin involved in innate immunity. Agglutinates all types of human erythrocytes, Gram-positive and Gram-negative bacteria. Has a stronger agglutinating activity towards Gram-negative bacteria than towards Gram-positive bacteria. Specifically recognizes acetyl group-containing substances on agglutinated cells. The hemagglutinating activity was inhibited by EDTA, acetyl group-containing mono- and disaccharides, N-acetyl derivatives of amino acids, other acetyl group-containing substances, propionamide and benzamide. Enhances the antimicrobial activity of big defensin against Gram-positive bacteria but not against Gram-negative bacteria.<ref>PMID:10468566</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1jc9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1jc9

From Proteopedia

Revision as of 00:11, 12 September 2015

TACHYLECTIN 5A FROM TACHYPLEUS TRIDENTATUS (JAPANESE HORSESHOE CRAB)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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