3fxy

From Proteopedia

(Difference between revisions)

Current revision

Acidic Mammalian Chinase, Catalytic Domain

Structural highlights

3fxy is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHIA_HUMAN 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.^[1] ^[2] ^[3] ^[4]

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

Acidic mammalian chitinase (AMCase) is a mammalian chitinase that has been implicated in allergic asthma. One of only two active mammalian chinases, AMCase, is distinguished from other chitinases by several unique features. Here, we present the novel structure of the AMCase catalytic domain, both in the apo form and in complex with the inhibitor methylallosamidin, determined to high resolution by X-ray crystallography. These results provide a structural basis for understanding some of the unique characteristics of this enzyme, including the low pH optimum and the preference for the beta-anomer of the substrate. A triad of polar residues in the second-shell is found to modulate the highly conserved chitinase active site. As a novel target for asthma therapy, structural details of AMCase activity will help guide the future design of specific and potent AMCase inhibitors.

Triad of polar residues implicated in pH specificity of acidic mammalian chitinase.,Olland AM, Strand J, Presman E, Czerwinski R, Joseph-McCarthy D, Krykbaev R, Schlingmann G, Chopra R, Lin L, Fleming M, Kriz R, Stahl M, Somers W, Fitz L, Mosyak L Protein Sci. 2009 Mar;18(3):569-78. PMID:19241384^[5]

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

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:http://dx.doi.org/10.1074/jbc.M009886200
↑ Hartl D, He CH, Koller B, Da Silva CA, Homer R, Lee CG, Elias JA. Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells. J Biol Chem. 2008 Nov 28;283(48):33472-82. doi: 10.1074/jbc.M805574200. Epub 2008, Sep 29. PMID:18824549 doi:http://dx.doi.org/10.1074/jbc.M805574200
↑ Hartl D, He CH, Koller B, Da Silva CA, Kobayashi Y, Lee CG, Flavell RA, Elias JA. Acidic mammalian chitinase regulates epithelial cell apoptosis via a chitinolytic-independent mechanism. J Immunol. 2009 Apr 15;182(8):5098-106. doi: 10.4049/jimmunol.0803446. PMID:19342690 doi:http://dx.doi.org/10.4049/jimmunol.0803446
↑ Seibold MA, Reese TA, Choudhry S, Salam MT, Beckman K, Eng C, Atakilit A, Meade K, Lenoir M, Watson HG, Thyne S, Kumar R, Weiss KB, Grammer LC, Avila P, Schleimer RP, Fahy JV, Rodriguez-Santana J, Rodriguez-Cintron W, Boot RG, Sheppard D, Gilliland FD, Locksley RM, Burchard EG. Differential enzymatic activity of common haplotypic versions of the human acidic Mammalian chitinase protein. J Biol Chem. 2009 Jul 17;284(29):19650-8. doi: 10.1074/jbc.M109.012443. Epub 2009, May 12. PMID:19435888 doi:http://dx.doi.org/10.1074/jbc.M109.012443
↑ Olland AM, Strand J, Presman E, Czerwinski R, Joseph-McCarthy D, Krykbaev R, Schlingmann G, Chopra R, Lin L, Fleming M, Kriz R, Stahl M, Somers W, Fitz L, Mosyak L. Triad of polar residues implicated in pH specificity of acidic mammalian chitinase. Protein Sci. 2009 Mar;18(3):569-78. PMID:19241384 doi:http://dx.doi.org/10.1002/pro.63

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fxy"

Categories: Homo sapiens | Large Structures | Olland AM

@@ Line 3: / Line 3: @@
 <StructureSection load='3fxy' size='340' side='right'caption='[[3fxy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3fxy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FXY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fxy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FXY FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fy1|3fy1]]</div></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]] 2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHIA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></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=3fxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxy OCA], [https://pdbe.org/3fxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fxy RCSB], [https://www.ebi.ac.uk/pdbsum/3fxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fxy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CHIA_HUMAN CHIA_HUMAN]] 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.<ref>PMID:11085997</ref> <ref>PMID:18824549</ref> <ref>PMID:19342690</ref> <ref>PMID:19435888</ref>
+[https://www.uniprot.org/uniprot/CHIA_HUMAN CHIA_HUMAN] 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.<ref>PMID:11085997</ref> <ref>PMID:18824549</ref> <ref>PMID:19342690</ref> <ref>PMID:19435888</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/3fxy_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 37: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Chitinase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Olland, A M]]
+[[Category: Olland AM]]
-[[Category: Alternative splicing]]
-[[Category: Asthma]]
-[[Category: Carbohydrate metabolism]]
-[[Category: Chitin degradation]]
-[[Category: Chitin-binding]]
-[[Category: Cytoplasm]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Polymorphism]]
-[[Category: Polysaccharide degradation]]
-[[Category: Secreted]]

3fxy

From Proteopedia

Current revision

Acidic Mammalian Chinase, Catalytic Domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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