1hjv

From Proteopedia

(Difference between revisions)

Revision as of 00:36, 10 September 2015

Crystal structure of hcgp-39 in complex with chitin tetramer

Structural highlights

1hjv 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.
Ligands:	,
Related:	1hjw, 1hjx
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Disease

[CH3L1_HUMAN] A genetic variation in CHI3L1 is associated with susceptibility to asthma-related traits type 7 (ASRT7) [MIM:611960]. Asthma-related traits include clinical symptoms of asthma, such as coughing, wheezing and dyspnea, bronchial hyperresponsiveness (BHR) as assessed by methacholine challenge test, serum IgE levels, atopy, and atopic dermatitis.

Function

[CH3L1_HUMAN] Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment.^[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

The 39-kDa human cartilage glycoprotein (HCGP39), a member of a novel family of chitinase-like lectins (Chilectins), is overexpressed in articular chondrocytes and certain cancers. Proposed functions of this protein include a role in connective tissue remodeling and defense against pathogens. Similar to other Chi-lectins, HCGP39 promotes the growth of connective tissue cells. The ability of HCGP39 to activate cytoplasmic signaling pathways suggests the presence of a ligand for this protein at the cell surface. There is currently no information regarding the identity of any physiological or pathological ligands of the Chi-lectins or the nature of the protein-ligand interaction. Here, we show that HCGP39 is able to bind chitooligosaccharides with micromolar affinity. Crystal structures of the native protein and a complex with GlcNAc8 show that the ligand is bound in identical fashion to family 18 chitinases. However, unlike the chitinases, binding of the oligosaccharide ligand to HCGP39 induces a large conformational change. Thus, HCGP39 could be a lectin that binds chitin-like oligosaccharide ligands and possibly plays a role in innate responses to chitinous pathogens, such as fungi and nematodes.

Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes.,Houston DR, Recklies AD, Krupa JC, van Aalten DM J Biol Chem. 2003 Aug 8;278(32):30206-12. Epub 2003 May 29. PMID:12775711^[2]

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

References

↑ Renkema GH, Boot RG, Au FL, Donker-Koopman WE, Strijland A, Muijsers AO, Hrebicek M, Aerts JM. Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages. Eur J Biochem. 1998 Jan 15;251(1-2):504-9. PMID:9492324
↑ Houston DR, Recklies AD, Krupa JC, van Aalten DM. Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes. J Biol Chem. 2003 Aug 8;278(32):30206-12. Epub 2003 May 29. PMID:12775711 doi:10.1074/jbc.M303371200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hjw|1hjw]], [[1hjx|1hjx]]</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=1hjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hjv RCSB], [http://www.ebi.ac.uk/pdbsum/1hjv 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=1hjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjv OCA], [http://pdbe.org/1hjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hjv RCSB], [http://www.ebi.ac.uk/pdbsum/1hjv PDBsum]</span></td></tr>
 </table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/CH3L1_HUMAN CH3L1_HUMAN]] A genetic variation in CHI3L1 is associated with susceptibility to asthma-related traits type 7 (ASRT7) [MIM:[http://omim.org/entry/611960 611960]]. Asthma-related traits include clinical symptoms of asthma, such as coughing, wheezing and dyspnea, bronchial hyperresponsiveness (BHR) as assessed by methacholine challenge test, serum IgE levels, atopy, and atopic dermatitis.
+== Function ==
+[[http://www.uniprot.org/uniprot/CH3L1_HUMAN CH3L1_HUMAN]] Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment.<ref>PMID:9492324</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1hjv" style="background-color:#fffaf0;"></div>
 ==See Also==

1hjv

From Proteopedia

Revision as of 00:36, 10 September 2015

Crystal structure of hcgp-39 in complex with chitin tetramer

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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