4rd9: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==X-RAY STRUCTURE OF THE APO FORM OF THE AMYLOID PRECURSOR PROTEIN-LIKE PROTEIN 1 (APLP1) E2 DOMAIN== | ||
<StructureSection load='4rd9' size='340' side='right' caption='[[4rd9]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4rd9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RD9 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=4rd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rd9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rd9 RCSB], [http://www.ebi.ac.uk/pdbsum/4rd9 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[ | [[http://www.uniprot.org/uniprot/APLP1_HUMAN APLP1_HUMAN]] May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis. | ||
[[Category: Dahms, S | __TOC__ | ||
[[Category: Than, M | </StructureSection> | ||
[[Category: Dahms, S O]] | |||
[[Category: Than, M E]] | |||
[[Category: Heparin binding]] | |||
[[Category: Sugar binding protein]] | |||
Revision as of 11:56, 11 March 2015
X-RAY STRUCTURE OF THE APO FORM OF THE AMYLOID PRECURSOR PROTEIN-LIKE PROTEIN 1 (APLP1) E2 DOMAIN
| ||||||||||||
