2dm4: Difference between revisions
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==Solution structure of the second fn3 domain of human sorLA/LR11== | ==Solution structure of the second fn3 domain of human sorLA/LR11== | ||
<StructureSection load='2dm4' size='340' side='right' caption='[[2dm4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2dm4' size='340' side='right'caption='[[2dm4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dm4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2dm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DM4 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SORL1 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SORL1 ([https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dm4 OCA], [https://pdbe.org/2dm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dm4 RCSB], [https://www.ebi.ac.uk/pdbsum/2dm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dm4 ProSAT], [https://www.topsan.org/Proteins/RSGI/2dm4 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SORL_HUMAN SORL_HUMAN]] Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction. | ||
== 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: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Hayashi, F]] | [[Category: Hayashi, F]] | ||
[[Category: Kurosaki, C]] | [[Category: Kurosaki, C]] | ||
Revision as of 12:07, 3 February 2021
Solution structure of the second fn3 domain of human sorLA/LR11
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Human
- Large Structures
- Hayashi, F
- Kurosaki, C
- Nagashima, T
- Structural genomic
- Yokoyama, S
- Yoshida, M
- Alzheimer's disease
- App
- Bace1
- Beta-sandwich
- Lipid transport
- Low-density lipoprotein receptor relative with 11 ligand-binding repeat
- Lr11
- National project on protein structural and functional analyse
- Nppsfa
- Rsgi
- Sorla
- Sorting protein-related receptor containing ldlr class a repeat
