8fra: Difference between revisions

Revision as of 06:22, 19 July 2023

Mouse acidic mammalian chitinase, catalytic domain in complex with diacetylchitobiose at pH 5.60

Structural highlights

8fra is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:	MG, NAG, NDG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHIA_MOUSE Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. Presence in saliva and gastric juice suggests a function as a digestive enzyme.^[1] ^[2] ^[3] ^[4]

References

↑ Boot RG, Blommaart EF, Swart E, Ghauharali-van der Vlugt K, Bijl N, Moe C, Place A, Aerts JM. Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem. 2001 Mar 2;276(9):6770-8. Epub 2000 Nov 20. PMID:11085997 doi:https://dx.doi.org/10.1074/jbc.M009886200
↑ Suzuki M, Fujimoto W, Goto M, Morimatsu M, Syuto B, Iwanaga T. Cellular expression of gut chitinase mRNA in the gastrointestinal tract of mice and chickens. J Histochem Cytochem. 2002 Aug;50(8):1081-9. PMID:12133911 doi:10.1177/002215540205000810
↑ Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, Hamid Q, Elias JA. Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science. 2004 Jun 11;304(5677):1678-82. PMID:15192232 doi:10.1126/science.1095336
↑ Chen L, Shen Z, Wu J. Expression, purification and in vitro antifungal activity of acidic mammalian chitinase against Candida albicans, Aspergillus fumigatus and Trichophyton rubrum strains. Clin Exp Dermatol. 2009 Jan;34(1):55-60. PMID:19076793 doi:10.1111/j.1365-2230.2008.03092.x

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OCA

[1] Boot RG, Blommaart EF, Swart E, Ghauharali-van der Vlugt K, Bijl N, Moe C, Place A, Aerts JM. Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem. 2001 Mar 2;276(9):6770-8. Epub 2000 Nov 20. PMID:11085997 doi:https://dx.doi.org/10.1074/jbc.M009886200

[2] Suzuki M, Fujimoto W, Goto M, Morimatsu M, Syuto B, Iwanaga T. Cellular expression of gut chitinase mRNA in the gastrointestinal tract of mice and chickens. J Histochem Cytochem. 2002 Aug;50(8):1081-9. PMID:12133911 doi:10.1177/002215540205000810

[3] Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, Hamid Q, Elias JA. Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science. 2004 Jun 11;304(5677):1678-82. PMID:15192232 doi:10.1126/science.1095336

[4] Chen L, Shen Z, Wu J. Expression, purification and in vitro antifungal activity of acidic mammalian chitinase against Candida albicans, Aspergillus fumigatus and Trichophyton rubrum strains. Clin Exp Dermatol. 2009 Jan;34(1):55-60. PMID:19076793 doi:10.1111/j.1365-2230.2008.03092.x

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[8fra]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FRA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fra OCA], [https://pdbe.org/8fra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fra RCSB], [https://www.ebi.ac.uk/pdbsum/8fra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fra ProSAT]</span></td></tr>
 </table>

8fra: Difference between revisions

Revision as of 06:22, 19 July 2023

Mouse acidic mammalian chitinase, catalytic domain in complex with diacetylchitobiose at pH 5.60

Structural highlights

Function

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