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1h20

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{{STRUCTURE_1h20| PDB=1h20 | SCENE= }}
{{STRUCTURE_1h20| PDB=1h20 | SCENE= }}
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'''SOLUTION STRUCTURE OF THE POTATO CARBOXYPEPTIDASE INHIBITOR'''
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===SOLUTION STRUCTURE OF THE POTATO CARBOXYPEPTIDASE INHIBITOR===
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==Overview==
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The solution structure and backbone dynamics of the recombinant potato carboxypeptidase inhibitor (PCI) have been characterized by NMR spectroscopy. The structure, determined on the basis of 497 NOE-derived distance constraints, is much better defined than the one reported in a previous NMR study, with an average pairwise backbone root-mean-square deviation of 0.5 A for the well-defined region of the protein, residues 7-37. Many of the side-chains show now well-defined conformations, both in the hydrophobic core and on the surface of the protein. Overall, the solution structure of free PCI is similar to the one that it shows in the crystal of the complex with carboxypeptidase A. However, some local differences are observed in regions 15-21 and 27-29. In solution, the six N-terminal and the two C-terminal residues are rather flexible, as shown by 15N backbone relaxation measurements. The flexibility of the latter segment may have implications in the binding of the inhibitor by the enzyme. All the remaining residues in the protein are essentially rigid (S2 &gt; 0.8) with the exception of two of them at the end of a short 3/10 helix. Despite the small size of the protein, a number of amide protons are protected from exchange with solvent deuterons. The slowest exchanging protons are those in a small two-strand beta-sheet. The unfolding free energies, as calculated from the exchange rates of these protons, are around 5 kcal/mol. Other protected amide protons are located in the segment 7-12, adjacent to the beta-sheet. Although these residues are not in an extended conformation in PCI, the equivalent residues in structurally homologous proteins form a third strand of the central beta-sheet. The amide protons in the 3/10 helix are only marginally protected, indicating that they exchange by a local unfolding mechanism, which is consistent with the increase in flexibility shown by some of its residues. Backbone alignment-based programs for folding recognition, as opposite to disulfide-bond alignments, reveal new proteins of unrelated sequence and function with a similar structure.
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(as it appears on PubMed at http://www.pubmed.gov), where 12557184 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12557184}}
==About this Structure==
==About this Structure==
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1H20 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H20 OCA].
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1H20 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H20 OCA].
==Reference==
==Reference==
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[[Category: Metalloenzyme inhibitor]]
[[Category: Metalloenzyme inhibitor]]
[[Category: Plant defense]]
[[Category: Plant defense]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:19:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:29:15 2008''

Revision as of 03:29, 1 July 2008

Image:1h20.png

Template:STRUCTURE 1h20

SOLUTION STRUCTURE OF THE POTATO CARBOXYPEPTIDASE INHIBITOR

Template:ABSTRACT PUBMED 12557184

About this Structure

1H20 is a Single protein structure of sequence from Solanum tuberosum. Full experimental information is available from OCA.

Reference

Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR., Gonzalez C, Neira JL, Ventura S, Bronsoms S, Rico M, Aviles FX, Proteins. 2003 Feb 15;50(3):410-22. PMID:12557184

Page seeded by OCA on Tue Jul 1 06:29:15 2008

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