2v1v

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[[Image:2v1v.jpg|left|200px]]
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{{STRUCTURE_2v1v| PDB=2v1v | SCENE= }}
{{STRUCTURE_2v1v| PDB=2v1v | SCENE= }}
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'''3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I'''
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===3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I===
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==Overview==
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Protein molecules can accommodate a large number of mutations without noticeable effects on their stability and folding kinetics. On the other hand, some mutations can have quite strong effects on protein conformational properties. Such mutations either destabilize secondary structures, e.g., alpha-helices, are incompatible with close packing of protein hydrophobic cores, or lead to disruption of some specific interactions such as disulfide cross links, salt bridges, hydrogen bonds, or aromatic-aromatic contacts. The Met8 --&gt; Leu mutation in CMTI-I results in significant destabilization of the protein structure. This effect could hardly be expected since the mutation is highly conservative, and the side chain of residue 8 is situated on the protein surface. We show that the protein destabilization is caused by rearrangement of a hydrophobic cluster formed by side chains of residues 8, Ile6, and Leu17 that leads to partial breaking of a hydrogen bond formed by the amide group of Leu17 with water and to a reduction of a hydrophobic surface buried within the cluster. The mutation perturbs also the protein folding. In aerobic conditions the reduced wild-type protein folds effectively into its native structure, whereas more then 75% of the mutant molecules are trapped in various misfolded species. The main conclusion of this work is that conservative mutations of hydrophobic residues can destabilize a protein structure even if these residues are situated on the protein surface and partially accessible to water. Structural rearrangement of small hydrophobic clusters formed by such residues can lead to local changes in protein hydration, and consequently, can affect considerably protein stability and folding process.
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The line below this paragraph, {{ABSTRACT_PUBMED_10716179}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10716179 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10716179}}
==About this Structure==
==About this Structure==
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2V1V is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bxj 1bxj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1V OCA].
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2V1V is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bxj 1bxj]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1V OCA].
==Reference==
==Reference==
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[[Category: Serine protease inhibitor]]
[[Category: Serine protease inhibitor]]
[[Category: Trypsin inhibitor]]
[[Category: Trypsin inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:03:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:01:35 2008''

Revision as of 07:01, 29 July 2008

Image:2v1v.png

Template:STRUCTURE 2v1v

3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I

Template:ABSTRACT PUBMED 10716179

About this Structure

2V1V is a Single protein structure. This structure supersedes the now removed PDB entry 1bxj. Full experimental information is available from OCA.

Reference

Conservative mutation Met8 --> Leu affects the folding process and structural stability of squash trypsin inhibitor CMTI-I., Zhukov I, Jaroszewski L, Bierzynski A, Protein Sci. 2000 Feb;9(2):273-9. PMID:10716179

Page seeded by OCA on Tue Jul 29 10:01:35 2008

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