5tpt
From Proteopedia
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==The Crystal Structure of Amyloid Precursor-Like Protein 2 (APLP2) E2 Domain== | ==The Crystal Structure of Amyloid Precursor-Like Protein 2 (APLP2) E2 Domain== | ||
| - | <StructureSection load='5tpt' size='340' side='right' caption='[[5tpt]], [[Resolution|resolution]] 2.42Å' scene=''> | + | <StructureSection load='5tpt' size='340' side='right'caption='[[5tpt]], [[Resolution|resolution]] 2.42Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5tpt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TPT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TPT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tpt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TPT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TPT FirstGlance]. <br> |
| - | </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=5tpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tpt OCA], [http://pdbe.org/5tpt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tpt RCSB], [http://www.ebi.ac.uk/pdbsum/5tpt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tpt ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APLP2, APPL2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5tpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tpt OCA], [http://pdbe.org/5tpt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tpt RCSB], [http://www.ebi.ac.uk/pdbsum/5tpt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tpt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/APLP2_HUMAN APLP2_HUMAN]] May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity).<ref>PMID:8307156</ref> | [[http://www.uniprot.org/uniprot/APLP2_HUMAN APLP2_HUMAN]] May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity).<ref>PMID:8307156</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The amyloid precursor-like protein 2 (APLP2) molecule is a type I transmembrane protein that is crucial for survival, cell-cell adhesion, neuronal development, myelination, cancer metastasis, modulation of metal, and glucose and insulin homeostasis. Moreover, the importance of the amyloid precursor protein (APP) family in biology and disease is very well known because of its central role in Alzheimer disease. In this study, we determined the crystal structure of the independently folded E2 domain of APLP2 and compared that with its paralogues APP and APLP2, demonstrating high overall structural similarities. The crystal structure of APLP2 E2 was solved as an antiparallel dimer, and analysis of the protein interfaces revealed a distinct mode of dimerization that differs from the previously reported dimerization of either APP or APLP1. Analysis of the APLP2 E2 metal binding sites suggested it binds zinc and copper in a similar manner to APP and APLP1. The structure of this key protein might suggest a relationship between the distinct mode of dimerization and its biologic functions.-Roisman, L. C., Han, S., Chuei, M. J., Connor, A. R., Cappai, R. The crystal structure of amyloid precursor-like protein 2 E2 domain completes the amyloid precursor protein family. | ||
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| + | The crystal structure of amyloid precursor-like protein 2 E2 domain completes the amyloid precursor protein family.,Roisman LC, Han S, Chuei MJ, Connor AR, Cappai R FASEB J. 2019 Apr;33(4):5076-5081. doi: 10.1096/fj.201802315R. Epub 2019 Jan 4. PMID:30608876<ref>PMID:30608876</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5tpt" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Cappai, R]] | [[Category: Cappai, R]] | ||
[[Category: Roisman, L C]] | [[Category: Roisman, L C]] | ||
Revision as of 06:29, 29 May 2019
The Crystal Structure of Amyloid Precursor-Like Protein 2 (APLP2) E2 Domain
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