This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2g41

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 14:39, 29 December 2021

Crystal structure of the complex of sheep signalling glycoprotein with chitin trimer at 3.0A resolution

Structural highlights

2g41 is a 1 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1r2v, 1zbk
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CH3L1_SHEEP] 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 (By similarity).

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

Crystal structures of four complexes of sheep secretory glycoprotein (SPS-40) with N-acetylglucosamine oligosaccharides (GlcNAc(n), (n=3-6)) have been determined at moderate resolutions. The binding studies of SPS-40 have been carried out using fluorescence spectroscopy and Surface Plasmon Resonance (SPR). Structure determinations of four complexes have shown a novel binding pattern of GlcNAc(n) molecules to SPS-40. The results indicate that the most preferred recognition region in the carbohydrate binding groove in SPS-40 is at subsites -4 to -2 among which subsite -2 provides the maximum interactions with carbohydrate residues. These structures have also shown that the interactions of GlcNAc3 and GlcNAc4 do not perturb the protein structure and those of GlcNAc5 induce partial conformational changes while in the case of GlcNAc6 the partially closed binding groove opened up completely. As in other SPX-40 structures, SPS-40 structure contains three overlapping flexible surface segments, His188-His197, Phe202-Arg212 and Phe244-Pro260 with several charged residues protruding outwardly. It creates a cluster of positive charges with a flexible base thus indicating a good scope of promoting the intermolecular interactions. This protein is glycosylated at Asn39 and may recognize other receptors having sugar binding sites. It appears that SPS-40 may involve both carbohydrate and protein bindings. The systematic carbohydrate-binding studies and the detailed structural results of four protein-carbohydrate complexes provide an excellent insight into the mechanism of carbohydrate binding. These are the first studies of this kind on secretory glycoproteins and their interactions with carbohydrates.

Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides.,Srivastava DB, Ethayathulla AS, Kumar J, Somvanshi RK, Sharma S, Dey S, Singh TP J Struct Biol. 2007 Jun;158(3):255-66. Epub 2006 Nov 17. PMID:17188513^[1]

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

References

↑ Srivastava DB, Ethayathulla AS, Kumar J, Somvanshi RK, Sharma S, Dey S, Singh TP. Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides. J Struct Biol. 2007 Jun;158(3):255-66. Epub 2006 Nov 17. PMID:17188513 doi:http://dx.doi.org/10.1016/j.jsb.2006.11.002

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/2g41"

@@ Line 3: / Line 3: @@
 <StructureSection load='2g41' size='340' side='right'caption='[[2g41]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2g41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G41 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2g41]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G41 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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">[[1r2v|1r2v]], [[1zbk|1zbk]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r2v|1r2v]], [[1zbk|1zbk]]</div></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=2g41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g41 OCA], [http://pdbe.org/2g41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g41 RCSB], [http://www.ebi.ac.uk/pdbsum/2g41 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2g41 ProSAT]</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=2g41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g41 OCA], [https://pdbe.org/2g41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g41 RCSB], [https://www.ebi.ac.uk/pdbsum/2g41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g41 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CH3L1_SHEEP CH3L1_SHEEP]] 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 (By similarity).
+[[https://www.uniprot.org/uniprot/CH3L1_SHEEP CH3L1_SHEEP]] 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 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2g41

From Proteopedia

Revision as of 14:39, 29 December 2021

Crystal structure of the complex of sheep signalling glycoprotein with chitin trimer at 3.0A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox