|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5xep' size='340' side='right'caption='[[5xep]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5xep' size='340' side='right'caption='[[5xep]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xep]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XEP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XEP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xep]] is a 6 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=5XEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XEP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xep OCA], [http://pdbe.org/5xep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xep RCSB], [http://www.ebi.ac.uk/pdbsum/5xep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xep ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5xep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xep OCA], [https://pdbe.org/5xep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xep RCSB], [https://www.ebi.ac.uk/pdbsum/5xep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xep ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CH3L1_MOUSE CH3L1_MOUSE]] Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.<ref>PMID:16472595</ref> <ref>PMID:19041398</ref> <ref>PMID:19414556</ref> <ref>PMID:20558631</ref> <ref>PMID:21546314</ref> <ref>PMID:22817986</ref> | + | [https://www.uniprot.org/uniprot/CH3L1_MOUSE CH3L1_MOUSE] Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.<ref>PMID:16472595</ref> <ref>PMID:19041398</ref> <ref>PMID:19414556</ref> <ref>PMID:20558631</ref> <ref>PMID:21546314</ref> <ref>PMID:22817986</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Breast regression protein (BRP39) is a glycoprotein, which is expressed during mammary gland involution in mouse. The physiological function of BRP39 is not known. High levels of expression of BRP39 have also been associated with breast cancer development. In the present investigation a cDNA encoding rBRP39 (recombinant BRP39) was cloned by PCR techniques. It consists of 1,143 nucleotides and encodes an open reading frame of 381 amino acid residues including a signal sequence of 21 amino acids. Recombinant BRP39 was produced in E. coli in a soluble form at low temperature (15 degrees C). Expression and purification of rBRP39 was confirmed by western blot analysis. Purified rBRP39 showed high chitin-binding activity but no chitinase activity. The lack of chitinase activity may be attributed to the mutation of critical active site residue Glu120 to Leu120 and Asp118 to Ala118 in BRP39. However, a mutant in which the residue was reverted back to Glu, by site directed mutagenesis, displayed no chitinase activity. Purified recombinant BRP39 was crystallized and the crystals diffracted X-rays to 2.8A resolution. The crystals belonged to the space group C2 with unit cell parameters a=130.4A, b=81.3A, c=229.2A, beta=105.9 degrees. The structure refinement is in progress.
| + | |
| - | | + | |
| - | Cloning, expression, characterization and crystallization of BRP39, a signalling glycoprotein expressed during mammary gland apoptosis.,Mohanty AK, Fisher AJ, Yu Z, Pradeep MA, Janjanam J, Kaushik JK Protein Expr Purif. 2009 Apr;64(2):213-8. doi: 10.1016/j.pep.2008.11.001. Epub, 2008 Nov 12. PMID:19041398<ref>PMID:19041398</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5xep" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| Line 26: |
Line 18: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Choudhary, S]] | + | [[Category: Mus musculus]] |
| - | [[Category: Fisher, A J]] | + | [[Category: Choudhary S]] |
| - | [[Category: Kaushik, J K]] | + | [[Category: Fisher AJ]] |
| - | [[Category: Mohanty, A K]] | + | [[Category: Kaushik JK]] |
| - | [[Category: Apoptosis]] | + | [[Category: Mohanty AK]] |
| - | [[Category: Sugar binding protein]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
CH3L1_MOUSE Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.[1] [2] [3] [4] [5] [6]
See Also
References
- ↑ Mizoguchi E. Chitinase 3-like-1 exacerbates intestinal inflammation by enhancing bacterial adhesion and invasion in colonic epithelial cells. Gastroenterology. 2006 Feb;130(2):398-411. doi: 10.1053/j.gastro.2005.12.007. PMID:16472595 doi:http://dx.doi.org/10.1053/j.gastro.2005.12.007
- ↑ Mohanty AK, Fisher AJ, Yu Z, Pradeep MA, Janjanam J, Kaushik JK. Cloning, expression, characterization and crystallization of BRP39, a signalling glycoprotein expressed during mammary gland apoptosis. Protein Expr Purif. 2009 Apr;64(2):213-8. doi: 10.1016/j.pep.2008.11.001. Epub, 2008 Nov 12. PMID:19041398 doi:http://dx.doi.org/10.1016/j.pep.2008.11.001
- ↑ Lee CG, Hartl D, Lee GR, Koller B, Matsuura H, Da Silva CA, Sohn MH, Cohn L, Homer RJ, Kozhich AA, Humbles A, Kearley J, Coyle A, Chupp G, Reed J, Flavell RA, Elias JA. Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in Th2 and IL-13-induced tissue responses and apoptosis. J Exp Med. 2009 May 11;206(5):1149-66. doi: 10.1084/jem.20081271. Epub 2009 May, 4. PMID:19414556 doi:http://dx.doi.org/10.1084/jem.20081271
- ↑ Sohn MH, Kang MJ, Matsuura H, Bhandari V, Chen NY, Lee CG, Elias JA. The chitinase-like proteins breast regression protein-39 and YKL-40 regulate hyperoxia-induced acute lung injury. Am J Respir Crit Care Med. 2010 Oct 1;182(7):918-28. doi:, 10.1164/rccm.200912-1793OC. Epub 2010 Jun 17. PMID:20558631 doi:http://dx.doi.org/10.1164/rccm.200912-1793OC
- ↑ Chen CC, Llado V, Eurich K, Tran HT, Mizoguchi E. Carbohydrate-binding motif in chitinase 3-like 1 (CHI3L1/YKL-40) specifically activates Akt signaling pathway in colonic epithelial cells. Clin Immunol. 2011 Sep;140(3):268-75. doi: 10.1016/j.clim.2011.04.007. Epub 2011 , Apr 20. PMID:21546314 doi:http://dx.doi.org/10.1016/j.clim.2011.04.007
- ↑ Dela Cruz CS, Liu W, He CH, Jacoby A, Gornitzky A, Ma B, Flavell R, Lee CG, Elias JA. Chitinase 3-like-1 promotes Streptococcus pneumoniae killing and augments host tolerance to lung antibacterial responses. Cell Host Microbe. 2012 Jul 19;12(1):34-46. doi: 10.1016/j.chom.2012.05.017. PMID:22817986 doi:http://dx.doi.org/10.1016/j.chom.2012.05.017
|
