2bkf: Difference between revisions
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==Structure of the PB1 domain of NBR1== | |||
<StructureSection load='2bkf' size='340' side='right'caption='[[2bkf]], [[Resolution|resolution]] 1.56Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bkf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BKF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2bkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkf OCA], [https://pdbe.org/2bkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bkf RCSB], [https://www.ebi.ac.uk/pdbsum/2bkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bkf ProSAT]</span></td></tr> | |||
</table> | |||
''' | == Function == | ||
[https://www.uniprot.org/uniprot/NBR1_HUMAN NBR1_HUMAN] Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets.<ref>PMID:19250911</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== | == Publication Abstract from PubMed == | ||
The scaffold protein NBR1 is involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Its N-terminal Phox and Bem1p (PB1) domain plays a critical role in mediating protein-protein interactions with both titin kinase and with another scaffold protein, p62. We have determined the crystal structure of the PB1 domain of NBR1 at 1.55A resolution. It reveals a type-A PB1 domain with two negatively charged residue clusters. We provide a structural perspective on the involvement of NBR1 in the titin kinase signalling pathway. | The scaffold protein NBR1 is involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Its N-terminal Phox and Bem1p (PB1) domain plays a critical role in mediating protein-protein interactions with both titin kinase and with another scaffold protein, p62. We have determined the crystal structure of the PB1 domain of NBR1 at 1.55A resolution. It reveals a type-A PB1 domain with two negatively charged residue clusters. We provide a structural perspective on the involvement of NBR1 in the titin kinase signalling pathway. | ||
Crystal structure of the PB1 domain of NBR1.,Muller S, Kursula I, Zou P, Wilmanns M FEBS Lett. 2006 Jan 9;580(1):341-4. Epub 2005 Dec 19. PMID:16376336<ref>PMID:16376336</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bkf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Kursula | [[Category: Kursula I]] | ||
[[Category: Mueller | [[Category: Mueller S]] | ||
[[Category: Wilmanns | [[Category: Wilmanns M]] | ||
Latest revision as of 09:17, 9 May 2024
Structure of the PB1 domain of NBR1
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