2v1v

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[[Image:2v1v.jpg|left|200px]]
 
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==3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I==
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The line below this paragraph, containing "STRUCTURE_2v1v", creates the "Structure Box" on the page.
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<StructureSection load='2v1v' size='340' side='right'caption='[[2v1v]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2v1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. 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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V1V FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1v OCA], [https://pdbe.org/2v1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v1v RCSB], [https://www.ebi.ac.uk/pdbsum/2v1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1v ProSAT]</span></td></tr>
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{{STRUCTURE_2v1v| PDB=2v1v | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ITR1_CUCMA ITR1_CUCMA] Inhibits trypsin.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I'''
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Conservative mutation Met8 --&gt; 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<ref>PMID:10716179</ref>
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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<div class="pdbe-citations 2v1v" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Conservative mutation Met8 --&gt; 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:[http://www.ncbi.nlm.nih.gov/pubmed/10716179 10716179]
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*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
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[[Category: Single protein]]
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== References ==
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[[Category: Bierzynski, A.]]
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<references/>
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[[Category: Bolewska, K.]]
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__TOC__
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[[Category: Sledz, P.]]
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</StructureSection>
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[[Category: Zhukov, I.]]
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[[Category: Cucurbita maxima]]
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[[Category: Hydrolase inhibitor hydrolase]]
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[[Category: Large Structures]]
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[[Category: Protease inhibitor]]
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[[Category: Bierzynski A]]
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[[Category: Serine protease inhibitor]]
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[[Category: Bolewska K]]
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[[Category: Trypsin inhibitor]]
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[[Category: Sledz P]]
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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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[[Category: Zhukov I]]

Current revision

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

PDB ID 2v1v

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