1b08: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b08]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B08 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B08 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1b08]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B08 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B08 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b08 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b08 RCSB], [http://www.ebi.ac.uk/pdbsum/1b08 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=1b08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b08 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b08 RCSB], [http://www.ebi.ac.uk/pdbsum/1b08 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hakansson, K | [[Category: Hakansson, K]] | ||
[[Category: Hoppe, H J | [[Category: Hoppe, H J]] | ||
[[Category: Lim, N K | [[Category: Lim, N K]] | ||
[[Category: Reid, K B.M | [[Category: Reid, K B.M]] | ||
[[Category: Alpha-helical coiled-coil]] | [[Category: Alpha-helical coiled-coil]] | ||
[[Category: C-type lectin]] | [[Category: C-type lectin]] | ||
Revision as of 12:18, 22 December 2014
LUNG SURFACTANT PROTEIN D (SP-D) (FRAGMENT)LUNG SURFACTANT PROTEIN D (SP-D) (FRAGMENT)
Structural highlights
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 PubMedBACKGROUND: Human lung surfactant protein D (hSP-D) belongs to the collectin family of C-type lectins and participates in the innate immune surveillance against microorganisms in the lung through recognition of carbohydrate ligands present on the surface of pathogens. The involvement of this protein in innate immunity and the allergic response make it the subject of much interest. RESULTS: We have determined the crystal structure of a trimeric fragment of hSP-D at 2.3 A resolution. The structure comprises an alpha-helical coiled-coil and three carbohydrate-recognition domains (CRDs). An interesting deviation from symmetry was found in the projection of a single tyrosine sidechain into the centre of the coiled-coil; the asymmetry of this residue influences the orientation of one of the adjacent CRDs. The cleft between the three CRDs presents a large positively charged surface. CONCLUSIONS: The fold of the CRD of hSP-D is similar to that of the mannan-binding protein (MBP), but its orientation relative to the alpha-helical coiled-coil region differs somewhat to that seen in the MBP structure. The novel central packing of the tyrosine sidechain within the coiled-coil and the resulting asymmetric orientation of the CRDs has unexpected functional implications. The positively charged surface might facilitate binding to negatively charged structures, such as lipopolysaccharides. Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin domains of human lung surfactant protein D.,Hakansson K, Lim NK, Hoppe HJ, Reid KB Structure. 1999 Mar 15;7(3):255-64. PMID:10368295[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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