5b3w: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5b3w is ~~ON HOLD~~ ~~until Paper~~ Publication

==Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in C2221 form==

== Structural highlights ==

<table><tr><td colspan='2'>[[5b3w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B3W FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b3x|5b3x]], [[5b3y|5b3y]], [[5b3z|5b3z]]</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=5b3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3w OCA], [http://pdbe.org/5b3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b3w RCSB], [http://www.ebi.ac.uk/pdbsum/5b3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3w ProSAT]</span></td></tr>

</table>

== Function ==

[[http://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>

== Publication Abstract from PubMed ==

Nascent proteins fold co-translationally because the folding speed and folding pathways are limited by the rate of ribosome biosynthesis in the living cell. In addition, though full-length proteins can fold all their residues during the folding process, nascent proteins initially fold only with the N-terminal residues. However, the transient structure and the co-translational folding pathway are not well understood. Here we report the atomic structures of a series of N-terminal fragments of the WW domain with increasing amino acid length. Unexpectedly, the structures indicate that the intermediate-length fragments take helical conformations even though the full-length protein has no helical regions. The circular dichroism spectra and theoretical calculations also support the crystallographic results. This suggests that the short-range interactions are more decisive in the structure formation than the long-range interactions for short nascent proteins. In the course of the peptide extension, the helical structure change to the structure mediated by the long-range interactions at a particular polypeptide length. Our results will provide unique information for elucidating the nature of co-translational folding.

~~Authors~~:

Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein.,Hanazono Y, Takeda K, Miki K Sci Rep. 2016 Oct 4;6:34654. doi: 10.1038/srep34654. PMID:27698466<ref>PMID:27698466</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Hanazono, Y]]

[[Category: Miki, K]]

[[Category: Takeda, K]]

[[Category: Isomerase]]

[[Category: Sugar binding protein]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5b3w is ON HOLD  until Paper Publication
+==Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in C2221 form==
+<StructureSection load='5b3w' size='340' side='right' caption='[[5b3w]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5b3w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B3W FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b3x|5b3x]], [[5b3y|5b3y]], [[5b3z|5b3z]]</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=5b3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3w OCA], [http://pdbe.org/5b3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b3w RCSB], [http://www.ebi.ac.uk/pdbsum/5b3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3w ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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 ==
+Nascent proteins fold co-translationally because the folding speed and folding pathways are limited by the rate of ribosome biosynthesis in the living cell. In addition, though full-length proteins can fold all their residues during the folding process, nascent proteins initially fold only with the N-terminal residues. However, the transient structure and the co-translational folding pathway are not well understood. Here we report the atomic structures of a series of N-terminal fragments of the WW domain with increasing amino acid length. Unexpectedly, the structures indicate that the intermediate-length fragments take helical conformations even though the full-length protein has no helical regions. The circular dichroism spectra and theoretical calculations also support the crystallographic results. This suggests that the short-range interactions are more decisive in the structure formation than the long-range interactions for short nascent proteins. In the course of the peptide extension, the helical structure change to the structure mediated by the long-range interactions at a particular polypeptide length. Our results will provide unique information for elucidating the nature of co-translational folding.
-Authors:
+Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein.,Hanazono Y, Takeda K, Miki K Sci Rep. 2016 Oct 4;6:34654. doi: 10.1038/srep34654. PMID:27698466<ref>PMID:27698466</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5b3w" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Hanazono, Y]]
+[[Category: Miki, K]]
+[[Category: Takeda, K]]
+[[Category: Isomerase]]
+[[Category: Sugar binding protein]]