View source for 9fvl


==Dimeric 14-3-3 zeta in complex with unphosphorylated MAP2c peptide==
<StructureSection load='9fvl' size='340' side='right'caption='[[9fvl]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fvl]] 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=9FVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FVL 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]] 2.08&#8491;</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></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=9fvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fvl OCA], [https://pdbe.org/9fvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fvl RCSB], [https://www.ebi.ac.uk/pdbsum/9fvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fvl 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9fvl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Jansen S]]
[[Category: Narasimhan S]]
[[Category: Zidek L]]