2v1v: Difference between revisions

Revision as of 10:01, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2v1v.png

Template:STRUCTURE 2v1v

3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I

Template:ABSTRACT PUBMED 10716179

About this StructureAbout this Structure

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

ReferenceReference

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2v1v|  PDB=2v1v  |  SCENE=  }}
-'''3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I'''
+===3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10716179}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10716179 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10716179}}
 ==About this Structure==
-V1V 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].
+V1V 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==
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 [[Category: Serine protease inhibitor]]
 [[Category: Trypsin inhibitor]]
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