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1zcn

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(New page: 200px<br /> <applet load="1zcn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zcn, resolution 1.9&Aring;" /> '''human Pin1 Ng mutant...)
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[[Image:1zcn.gif|left|200px]]<br /><applet load="1zcn" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1zcn" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1zcn, resolution 1.9&Aring;" />
caption="1zcn, resolution 1.9&Aring;" />
'''human Pin1 Ng mutant'''<br />
'''human Pin1 Ng mutant'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1ZCN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZCN OCA].
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1ZCN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCN OCA].
==Reference==
==Reference==
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[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bowman, M.E.]]
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[[Category: Bowman, M E.]]
[[Category: Dendel, G.]]
[[Category: Dendel, G.]]
[[Category: Gruebele, M.]]
[[Category: Gruebele, M.]]
[[Category: Jager, M.]]
[[Category: Jager, M.]]
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[[Category: Kelly, J.W.]]
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[[Category: Kelly, J W.]]
[[Category: Nguyen, H.]]
[[Category: Nguyen, H.]]
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[[Category: Noel, J.P.]]
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[[Category: Noel, J P.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
[[Category: 1PE]]
[[Category: 1PE]]
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[[Category: ww domain]]
[[Category: ww domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:32:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:14 2008''

Revision as of 14:14, 21 February 2008

Image:1zcn.gif

1zcn, resolution 1.9Å

Drag the structure with the mouse to rotate

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 with and as ligands. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 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 Thu Feb 21 16:14:14 2008

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