1zcn

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[[Image:1zcn.gif|left|200px]]
[[Image:1zcn.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1zcn |SIZE=350|CAPTION= <scene name='initialview01'>1zcn</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1zcn", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PIN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1zcn| PDB=1zcn | SCENE= }}
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|RELATEDENTRY=[[1pin|1pin]], [[1f8a|1f8a]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zcn OCA], [http://www.ebi.ac.uk/pdbsum/1zcn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zcn RCSB]</span>
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}}
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'''human Pin1 Ng mutant'''
'''human Pin1 Ng mutant'''
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[[Category: Noel, J P.]]
[[Category: Noel, J P.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
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[[Category: type i beta-turn]]
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[[Category: Type i beta-turn]]
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[[Category: ww domain]]
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[[Category: Ww domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:28:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:06 2008''
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Revision as of 14:28, 3 May 2008

Template:STRUCTURE 1zcn

human Pin1 Ng mutant


Overview

Protein folding barriers result from a combination of factors including unavoidable energetic frustration from nonnative interactions, natural variation and selection of the amino acid sequence for function, and/or selection pressure against aggregation. The rate-limiting step for human Pin1 WW domain folding is the formation of the loop 1 substructure. The native conformation of this six-residue loop positions side chains that are important for mediating protein-protein interactions through the binding of Pro-rich sequences. Replacement of the wild-type loop 1 primary structure by shorter sequences with a high propensity to fold into a type-I' beta-turn conformation or the statistically preferred type-I G1 bulge conformation accelerates WW domain folding by almost an order of magnitude and increases thermodynamic stability. However, loop engineering to optimize folding energetics has a significant downside: it effectively eliminates WW domain function according to ligand-binding studies. The energetic contribution of loop 1 to ligand binding appears to have evolved at the expense of fast folding and additional protein stability. Thus, the two-state barrier exhibited by the wild-type human Pin1 WW domain principally results from functional requirements, rather than from physical constraints inherent to even the most efficient loop formation process.

About this Structure

1ZCN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure-function-folding relationship in a WW domain., Jager M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW, Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10648-53. Epub 2006 Jun 28. PMID:16807295 Page seeded by OCA on Sat May 3 17:28:03 2008

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