5vtk: Difference between revisions

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'''Unreleased structure'''


The entry 5vtk is ON HOLD  until Paper Publication
==Structure of Pin1 WW Domain Variant 1 with beta3-Ser Loop Substitution==
<StructureSection load='5vtk' size='340' side='right'caption='[[5vtk]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vtk]] 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=5VTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VTK 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]] 1.99&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3S:(3R)-3-AMINO-4-HYDROXYBUTANOIC+ACID'>B3S</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5vtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vtk OCA], [https://pdbe.org/5vtk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vtk RCSB], [https://www.ebi.ac.uk/pdbsum/5vtk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vtk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Amino acids have a backbone that is expanded by one carbon atom relative to alpha-amino acids, and beta residues have been investigated as subunits in protein-like molecules that adopt discrete and predictable conformations. Two classes of beta residue have been widely explored in the context of generating alpha-helix-like conformations: beta(3) -amino acids, which are homologous to alpha-amino acids and bear a side chain on the backbone carbon adjacent to nitrogen, and residues constrained by a five-membered ring, such the one derived from trans-2-aminocyclopentanecarboxylic acid (ACPC). Substitution of alpha residues with their beta(3) homologues within an alpha-helix-forming sequence generally causes a decrease in conformational stability. Use of a ring-constrained beta residue, however, can offset the destabilizing effect of alpha--&gt;beta substitution. Here we extend the study of alpha--&gt;beta substitutions, involving both beta(3) and ACPC residues, to short loops within a small tertiary motif. We start from previously reported variants of the Pin1 WW domain that contain a two-, three-, or four-residue beta-hairpin loop, and we evaluate alpha--&gt;beta replacements at each loop position for each variant. By referral to the varphi,psi angles of the native structure, one can choose a stereochemically appropriate ACPC residue. Use of such logically chosen ACPC residues enhances conformational stability in several cases. Crystal structures of three beta-containing Pin1 WW domain variants show that a native-like tertiary structure is maintained in each case.


Authors: Mortenson, D.E., Kreitler, D.F., Thomas, N.C., Gellman, S.H., Forest, K.T.
Evaluation of beta-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.,Mortenson DE, Kreitler DF, Thomas NC, Guzei IA, Gellman SH, Forest KT Chembiochem. 2017 Dec 22. doi: 10.1002/cbic.201700580. PMID:29272560<ref>PMID:29272560</ref>


Description: Structure of Pin1 WW Domain Variant 1 with beta3-Ser Loop Substitution
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Mortenson, D.E]]
<div class="pdbe-citations 5vtk" style="background-color:#fffaf0;"></div>
[[Category: Kreitler, D.F]]
 
[[Category: Thomas, N.C]]
==See Also==
[[Category: Forest, K.T]]
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
[[Category: Gellman, S.H]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Forest KT]]
[[Category: Gellman SH]]
[[Category: Kreitler DF]]
[[Category: Mortenson DE]]
[[Category: Thomas NC]]
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