4m4d

From Proteopedia

(Difference between revisions)

Revision as of 10:54, 21 December 2022

Crystal structure of lipopolysaccharide binding protein

Structural highlights

4m4d is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LBP_MOUSE Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria, and acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity).

Publication Abstract from PubMed

Lipopolysaccharide (LPS) binding protein (LBP) is an acute-phase protein that initiates an immune response after recognition of bacterial LPS. Here, we report the crystal structure of murine LBP at 2.9 A resolution. Several structural differences were observed between LBP and the related bactericidal/permeability-increasing protein (BPI), and the LBP C-terminal domain contained a negatively charged groove and a hydrophobic "phenylalanine core." A frequent human LBP SNP (allelic frequency 0.08) affected this region, potentially generating a proteinase cleavage site. The mutant protein had a reduced binding capacity for LPS and lipopeptides. SNP carriers displayed a reduced cytokine response after in vivo LPS exposure and lower cytokine concentrations in pneumonia. In a retrospective trial, the LBP SNP was associated with increased mortality rates during sepsis and pneumonia. Thus, the structural integrity of LBP may be crucial for fighting infections efficiently, and future patient stratification might help to develop better therapeutic strategies.

The Crystal Structure of Lipopolysaccharide Binding Protein Reveals the Location of a Frequent Mutation that Impairs Innate Immunity.,Eckert JK, Kim YJ, Kim JI, Gurtler K, Oh DY, Sur S, Lundvall L, Hamann L, van der Ploeg A, Pickkers P, Giamarellos-Bourboulis E, Kubarenko AV, Weber AN, Kabesch M, Kumpf O, An HJ, Lee JO, Schumann RR Immunity. 2013 Oct 17;39(4):647-60. doi: 10.1016/j.immuni.2013.09.005. Epub 2013 , Oct 10. PMID:24120359^[1]

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

References

↑ Eckert JK, Kim YJ, Kim JI, Gurtler K, Oh DY, Sur S, Lundvall L, Hamann L, van der Ploeg A, Pickkers P, Giamarellos-Bourboulis E, Kubarenko AV, Weber AN, Kabesch M, Kumpf O, An HJ, Lee JO, Schumann RR. The Crystal Structure of Lipopolysaccharide Binding Protein Reveals the Location of a Frequent Mutation that Impairs Innate Immunity. Immunity. 2013 Oct 17;39(4):647-60. doi: 10.1016/j.immuni.2013.09.005. Epub 2013 , Oct 10. PMID:24120359 doi:http://dx.doi.org/10.1016/j.immuni.2013.09.005

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4m4d"

@@ Line 1: / Line 1: @@
 ==Crystal structure of lipopolysaccharide binding protein==
-<StructureSection load='4m4d' size='340' side='right' caption='[[4m4d]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
+<StructureSection load='4m4d' size='340' side='right'caption='[[4m4d]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4m4d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M4D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M4D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4m4d]] is a 2 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=4M4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M4D FirstGlance]. <br>
-</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=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Lbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4m4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4d OCA], [https://pdbe.org/4m4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m4d RCSB], [https://www.ebi.ac.uk/pdbsum/4m4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4d ProSAT]</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=4m4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4d OCA], [http://pdbe.org/4m4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m4d RCSB], [http://www.ebi.ac.uk/pdbsum/4m4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LBP_MOUSE LBP_MOUSE]] Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria, and acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity).
+[https://www.uniprot.org/uniprot/LBP_MOUSE LBP_MOUSE] Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria, and acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: An, H J]]
+[[Category: Mus musculus]]
-[[Category: Eckert, J K]]
+[[Category: An HJ]]
-[[Category: Giamarellos-Bourboulis, E]]
+[[Category: Eckert JK]]
-[[Category: Gurtler, K]]
+[[Category: Giamarellos-Bourboulis E]]
-[[Category: Hamann, L]]
+[[Category: Gurtler K]]
-[[Category: Kabesch, M]]
+[[Category: Hamann L]]
-[[Category: Kim, J I]]
+[[Category: Kabesch M]]
-[[Category: Kim, Y J]]
+[[Category: Kim JI]]
-[[Category: Kubarenko, A V]]
+[[Category: Kim YJ]]
-[[Category: Kumpf, O]]
+[[Category: Kubarenko AV]]
-[[Category: Lee, J O]]
+[[Category: Kumpf O]]
-[[Category: Lundvall, L]]
+[[Category: Lee JO]]
-[[Category: Oh, D Y]]
+[[Category: Lundvall L]]
-[[Category: Pickkers, P]]
+[[Category: Oh DY]]
-[[Category: Ploeg, A H]]
+[[Category: Pickkers P]]
-[[Category: Schumann, R R]]
+[[Category: Ploeg AH]]
-[[Category: Weber, A N]]
+[[Category: Schumann RR]]
-[[Category: Beta barrel]]
+[[Category: Weber AN]]
-[[Category: Blood]]
-[[Category: Immune response]]
-[[Category: Lipid binding protein]]
-[[Category: Lipopolysaccharide]]

4m4d

From Proteopedia

Revision as of 10:54, 21 December 2022

Crystal structure of lipopolysaccharide binding protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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