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| | <StructureSection load='3k6b' size='340' side='right'caption='[[3k6b]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='3k6b' size='340' side='right'caption='[[3k6b]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3k6b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3K6B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3k6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K6B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GU4:2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE'>GU4</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rw6|1rw6]], [[3k66|3k66]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GU4:2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE'>GU4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apl-1, C42D8.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=3k6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6b OCA], [https://pdbe.org/3k6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k6b RCSB], [https://www.ebi.ac.uk/pdbsum/3k6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6b ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3k6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6b OCA], [http://pdbe.org/3k6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k6b RCSB], [http://www.ebi.ac.uk/pdbsum/3k6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A4_CAEEL A4_CAEEL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ha, Y]] | + | [[Category: Ha Y]] |
| - | [[Category: Hoopes, J T]] | + | [[Category: Hoopes JT]] |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Amyloid]]
| + | |
| - | [[Category: Amyloid precursor protein]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Developmental protein]]
| + | |
| - | [[Category: Differentiation]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Heparin binding]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Neurogenesis]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: X-ray crystal structure]]
| + | |
| Structural highlights
Function
A4_CAEEL
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 amyloid beta-peptide deposit found in the brain tissue of patients with Alzheimer disease is derived from a large heparin-binding protein precursor APP. The biological function of APP and its homologs is not precisely known. Here we report the x-ray structure of the E2 domain of APL-1, an APP homolog in Caenorhabditis elegans, and compare it to the human APP structure. We also describe the structure of APL-1 E2 in complex with sucrose octasulfate, a highly negatively charged disaccharide, which reveals an unexpected binding pocket between the two halves of E2. Based on the crystal structure, we are able to map, using site-directed mutagenesis, a surface groove on E2 to which heparin may bind. Our biochemical data also indicate that the affinity of E2 for heparin is influenced by pH: at pH 5, the binding appears to be much stronger than that at neutral pH. This property is likely caused by histidine residues in the vicinity of the mapped heparin binding site and could be important for the proposed adhesive function of APL-1.
Structural characterization of the E2 domain of APL-1, a Caenorhabditis elegans homolog of human amyloid precursor protein, and its heparin binding site.,Hoopes JT, Liu X, Xu X, Demeler B, Folta-Stogniew E, Li C, Ha Y J Biol Chem. 2010 Jan 15;285(3):2165-73. Epub 2009 Nov 10. PMID:19906646[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hoopes JT, Liu X, Xu X, Demeler B, Folta-Stogniew E, Li C, Ha Y. Structural characterization of the E2 domain of APL-1, a Caenorhabditis elegans homolog of human amyloid precursor protein, and its heparin binding site. J Biol Chem. 2010 Jan 15;285(3):2165-73. Epub 2009 Nov 10. PMID:19906646 doi:10.1074/jbc.M109.018432
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