5jm4

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<StructureSection load='5jm4' size='340' side='right' caption='[[5jm4]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
<StructureSection load='5jm4' size='340' side='right' caption='[[5jm4]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jm4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JM4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jm4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JM4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=6L9:[(2S)-2,3-DIAMINO-3-OXOPROPYL]PROPANEDIOIC+ACID'>6L9</scene>, <scene name='pdbligand=A1G:(2S)-AMINO[(3R,5R,7R)-TRICYCLO[3.3.1.1~3,7~]DECAN-1-YL]ACETIC+ACID'>A1G</scene>, <scene name='pdbligand=MKD:(2S)-2-AMINO-2-METHYLOCTANOIC+ACID'>MKD</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=6L9:[(2S)-2,3-DIAMINO-3-OXOPROPYL]PROPANEDIOIC+ACID'>6L9</scene>, <scene name='pdbligand=A1G:(2S)-AMINO[(3R,5R,7R)-TRICYCLO[3.3.1.1~3,7~]DECAN-1-YL]ACETIC+ACID'>A1G</scene>, <scene name='pdbligand=MKD:(2S)-2-AMINO-2-METHYLOCTANOIC+ACID'>MKD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n7g|4n7g]], [[4n84|4n84]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n7g|4n7g]], [[4n84|4n84]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YWHAZ ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jm4 OCA], [http://pdbe.org/5jm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jm4 RCSB], [http://www.ebi.ac.uk/pdbsum/5jm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jm4 ProSAT]</span></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=5jm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jm4 OCA], [http://pdbe.org/5jm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jm4 RCSB], [http://www.ebi.ac.uk/pdbsum/5jm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jm4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[[http://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Macrocyclic peptides can interfere with challenging biomolecular targets including protein-protein interactions. Whereas there are various approaches that facilitate the identification of peptide-derived ligands, their evolution into higher affinity binders remains a major hurdle. We report a virtual screen based on molecular docking that allows the affinity maturation of macrocyclic peptides taking non-natural amino acids into consideration. These macrocycles bear large and flexible substituents that usually complicate the use of docking approaches. A virtual library containing more than 1400 structures was screened against the target focusing on docking poses with the core structure resembling a known bioactive conformation. Based on this screen, a macrocyclic peptide 22 involving two non-natural amino acids was evolved showing increased target affinity and biological activity. Predicted binding modes were verified by X-ray crystallography. The presented workflow allows the screening of large macrocyclic peptides with diverse modifications thereby expanding the accessible chemical space and reducing synthetic efforts.
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Structure-Based Design of Non-natural Macrocyclic Peptides That Inhibit Protein-Protein Interactions.,Kruger DM, Glas A, Bier D, Pospiech N, Wallraven K, Dietrich L, Ottmann C, Koch O, Hennig S, Grossmann TN J Med Chem. 2017 Nov 9;60(21):8982-8988. doi: 10.1021/acs.jmedchem.7b01221. Epub , 2017 Oct 27. PMID:29028171<ref>PMID:29028171</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5jm4" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[14-3-3 protein|14-3-3 protein]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Bier, D]]
[[Category: Bier, D]]
[[Category: Glas, A]]
[[Category: Glas, A]]

Revision as of 06:23, 24 October 2018

Crystal structure of 14-3-3zeta in complex with a cyclic peptide involving an adamantyl and a dicarboxy side chain

5jm4, resolution 2.34Å

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