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2v1v

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Revision as of 12:57, 5 August 2016

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

Structural highlights

2v1v is a 1 chain structure. This structure supersedes the now removed PDB entry 1bxj. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1bxj, 1cti, 1lu0, 1ppe, 2cti, 2sta, 3cti
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ITR1_CUCMA] Inhibits trypsin.

Publication Abstract from PubMed

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 --> 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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v1v"

@@ Line 1: / Line 1: @@
 ==3D STRUCTURE OF THE M8L MUTANT OF SQUASH TRYPSIN INHIBITOR CMTI-I==
 <StructureSection load='2v1v' size='340' side='right' caption='[[2v1v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2v1v]] is a 1 chain 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V1V FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bxj|1bxj]], [[1cti|1cti]], [[1lu0|1lu0]], [[1ppe|1ppe]], [[2cti|2cti]], [[2sta|2sta]], [[3cti|3cti]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v1v RCSB], [http://www.ebi.ac.uk/pdbsum/2v1v PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1v OCA], [http://pdbe.org/2v1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v1v RCSB], [http://www.ebi.ac.uk/pdbsum/2v1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1v ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2v1v" style="background-color:#fffaf0;"></div>
 ==See Also==

2v1v

From Proteopedia

Revision as of 12:57, 5 August 2016

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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