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2o9o

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Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution

Structural highlights

2o9o is a 1 chain structure with sequence from Bubalus bubalis. This structure supersedes the now removed PDB entry 1sv8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CH3L1_BUBBU 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

The crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 A resolution. SPB-40 acts as a protective signalling factor by binding to viable cells during the early phase of involution, during which extensive tissue remodelling occurs. It was isolated from the dry secretions of Murrah buffalo. It was purified and crystallized using the hanging-drop vapour-diffusion method with 19% ethanol as the precipitant. The protein was also cloned and its complete nucleotide and amino-acid sequences were determined. When compared with the sequences of other members of the family, the sequence of SPB-40 revealed two very important mutations in the sugar-binding region, in which Tyr120 changed to Trp120 and Glu269 changed to Trp269. The structure showed a significant distortion in the shape of the sugar-binding groove. The water structure in the groove is also drastically altered. The folding of the protein chain in the flexible region comprising segments His188-His197, Phe202-Arg212 and Tyr244-Pro260 shows large variations when compared with other proteins of the family.

Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution.,Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):258-65. Epub 2007 Mar 12. PMID:17401190^[1]

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

References

↑ Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP. Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):258-65. Epub 2007 Mar 12. PMID:17401190 doi:http://dx.doi.org/10.1107/S1744309107010445

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/2o9o"

@@ Line 3: / Line 3: @@
 <StructureSection load='2o9o' size='340' side='right'caption='[[2o9o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2o9o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bubbu Bubbu]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sv8 1sv8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O9O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2o9o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sv8 1sv8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O9O FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2esc|2esc]], [[2dpe|2dpe]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=2o9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o9o OCA], [http://pdbe.org/2o9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o9o RCSB], [http://www.ebi.ac.uk/pdbsum/2o9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o9o 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=2o9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o9o OCA], [https://pdbe.org/2o9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o9o RCSB], [https://www.ebi.ac.uk/pdbsum/2o9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o9o ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CH3L1_BUBBU CH3L1_BUBBU]] 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_BUBBU CH3L1_BUBBU] 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]]
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bubbu]]
+[[Category: Bubalus bubalis]]
 [[Category: Large Structures]]
-[[Category: Ethayathulla, A S]]
+[[Category: Ethayathulla AS]]
-[[Category: Kaur, P]]
+[[Category: Kaur P]]
-[[Category: Kumar, J]]
+[[Category: Kumar J]]
-[[Category: Sharma, S]]
+[[Category: Sharma S]]
-[[Category: Singh, T P]]
+[[Category: Singh TP]]
-[[Category: Srivastava, D B]]
+[[Category: Srivastava DB]]
-[[Category: Signaling protein]]
-[[Category: Spb-40]]
-[[Category: Tim barrel]]

2o9o

From Proteopedia

Current revision

Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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