9fum: Difference between revisions
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==Dimeric 14-3-3 zeta in complex with MAP2c peptide containing pS435== | |||
<StructureSection load='9fum' size='340' side='right'caption='[[9fum]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9fum]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FUM 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]] 2.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=9fum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fum OCA], [https://pdbe.org/9fum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fum RCSB], [https://www.ebi.ac.uk/pdbsum/9fum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fum ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Microtubule associated protein 2 (MAP2) interacts with the regulatory protein 14-3-3zeta in a cAMP-dependent protein kinase (PKA) phosphorylation dependent manner. Using selective phosphorylation, calorimetry, nuclear magnetic resonance, chemical crosslinking, and X-ray crystallography, we characterized interactions of 14-3-3zeta with various binding regions of MAP2c. Although PKA phosphorylation increases the affinity of MAP2c for 14-3-3zeta in the proline rich region and C-terminal domain, unphosphorylated MAP2c also binds the dimeric 14-3-3zeta via its microtubule binding domain and variable central domain. Monomerization of 14-3-3zeta leads to the loss of affinity for the unphosphorylated residues. In neuroblastoma cell extract, MAP2c is heavily phosphorylated by PKA and the proline kinase ERK2. Although 14-3-3zeta dimer or monomer do not interact with the residues phosphorylated by ERK2, ERK2 phosphorylation of MAP2c in the C-terminal domain reduces the binding of MAP2c to both oligomeric variants of 14-3-3zeta. | |||
Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14-3-3zeta.,Jansen S, Narasimhan S, Cabre Fernandez P, Ilkovicova L, Kozelekova A, Kralova K, Hritz J, Zidek L FEBS J. 2025 Jan 29. doi: 10.1111/febs.17405. PMID:39877981<ref>PMID:39877981</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9fum" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Zidek | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Jansen S]] | |||
[[Category: Narasimhan S]] | |||
[[Category: Zidek L]] | |||