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1pwb

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Revision as of 08:03, 24 February 2018

High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose

Structural highlights

1pwb is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1pw9, 1b08
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SFTPD_HUMAN] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.

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

Lung surfactant protein D (SP-D) can directly interact with carbohydrate residues on pulmonary pathogens and allergens, stimulate immune cells, and manipulate cytokine and chemokine profiles during the immune response in the lungs. Therapeutic administration of rfhSP-D, a recombinant homotrimeric fragment of human SP-D comprising the alpha-helical coiled-coil neck plus three CRDs, protects mice against lung allergy and infection caused by the fungal pathogen Aspergillus fumigatus. The high resolution crystal structures of maltose-bound rfhSP-D to 1.4A, and of rfhSP-D to 1.6A, define the fine detail of the mode and nature of carbohydrate recognition and provide insights into how a small fragment of human SP-D can bind to allergens/antigens or whole pathogens, and at the same time recruit and engage effector cells and molecules of humoral immunity. A previously unreported calcium ion, located on the trimeric axis in a pore at the bottom of the funnel formed by the three CRDs and close to the neck-CRD interface, is coordinated by a triad of glutamate residues which are, to some extent, neutralised by their interactions with a triad of exposed lysine residues in the funnel. The spatial relationship between the neck and the CRDs is maintained internally by these lysine residues, and externally by a glutamine, which forms a pair of hydrogen-bonds within an external cleft at each neck-CRD interface. Structural links between the central pore and the cleft suggest a possible effector mechanism for immune cell surface receptor binding in the presence of bound, extended natural lipopolysaccharide and phospholipid ligands. The structural requirements for such an effector mechanism, involving both the trimeric framework for multivalent ligand binding and recognition sites formed from more than one subunit, are present in both native hSP-D and rfhSP-D, providing a possible explanation for the significant biological activity of rfhSP-D.

High-resolution structural insights into ligand binding and immune cell recognition by human lung surfactant protein D.,Shrive AK, Tharia HA, Strong P, Kishore U, Burns I, Rizkallah PJ, Reid KB, Greenhough TJ J Mol Biol. 2003 Aug 8;331(2):509-23. PMID:12888356^[1]

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

References

↑ Shrive AK, Tharia HA, Strong P, Kishore U, Burns I, Rizkallah PJ, Reid KB, Greenhough TJ. High-resolution structural insights into ligand binding and immune cell recognition by human lung surfactant protein D. J Mol Biol. 2003 Aug 8;331(2):509-23. PMID:12888356

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose==
 <StructureSection load='1pwb' size='340' side='right' caption='[[1pwb]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pw9|1pw9]], [[1b08|1b08]]</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=1pwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pwb OCA], [http://pdbe.org/1pwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pwb RCSB], [http://www.ebi.ac.uk/pdbsum/1pwb 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=1pwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pwb OCA], [http://pdbe.org/1pwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pwb RCSB], [http://www.ebi.ac.uk/pdbsum/1pwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pwb ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pw/1pwb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pw/1pwb_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1pwb

From Proteopedia

Revision as of 08:03, 24 February 2018

High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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