2ci2
From Proteopedia
(New page: 200px<br /><applet load="2ci2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ci2, resolution 2.0Å" /> '''CRYSTAL AND MOLECULAR...) |
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| - | [[Image:2ci2.jpg|left|200px]]<br /><applet load="2ci2" size=" | + | [[Image:2ci2.jpg|left|200px]]<br /><applet load="2ci2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ci2, resolution 2.0Å" /> | caption="2ci2, resolution 2.0Å" /> | ||
'''CRYSTAL AND MOLECULAR STRUCTURE OF THE SERINE PROTEINASE INHIBITOR CI-2 FROM BARLEY SEEDS'''<br /> | '''CRYSTAL AND MOLECULAR STRUCTURE OF THE SERINE PROTEINASE INHIBITOR CI-2 FROM BARLEY SEEDS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley | + | Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley seeds, has been crystallized and its three-dimensional structure determined at 2.0-A resolution by the molecular replacement method. The structure has been refined by restrained-parameter least-squares methods to a crystallographic R factor (= sigma parallel Fo magnitude of-Fo parallel/sigma magnitude of Fo) o of 0.198. CI-2 is a member of the potato inhibitor 1 family. It lacks the characteristic stabilizing disulfide bonds of most other members of serine proteinase inhibitor families. The body of CI-2 shows few conformational changes between the free inhibitor and the previously reported structure of CI-2 in complex with subtilisin Novo [McPhalen, C.A., Svendsen, I., Jonassen, I., & James, M.N.G. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7242-7246]. However, the reactive site loop has some significant conformational differences between the free inhibitor and its complexed form. The residues in this segment of polypeptide exhibit relatively large thermal motion parameters and some disorder in the uncomplexed form of the inhibitor. The reactive site bond is between Met-59I and Glu-60I in the consecutive sequential numbering of CI-2 (Met-60-Glu-61 according to the alignment of Svendsen et al. [Svendsen, I., Hejgaard, J., & Chavan, J.K. (1984) Carlsberg Res. Commun. 49, 493-502]). The network of hydrogen bonds and electrostatic interactions stabilizing the conformation of the reactive site loop is much less extensive in the free than in the complexed inhibitor. |
==About this Structure== | ==About this Structure== | ||
| - | 2CI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. This structure | + | 2CI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. This structure supersedes the now removed PDB entry 1CI2. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: James, M | + | [[Category: James, M N.G.]] |
| - | [[Category: Mcphalen, C | + | [[Category: Mcphalen, C A.]] |
[[Category: proteinase inhibitor (chymotrypsin)]] | [[Category: proteinase inhibitor (chymotrypsin)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:58 2008'' |
Revision as of 14:48, 21 February 2008
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CRYSTAL AND MOLECULAR STRUCTURE OF THE SERINE PROTEINASE INHIBITOR CI-2 FROM BARLEY SEEDS
Overview
Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley seeds, has been crystallized and its three-dimensional structure determined at 2.0-A resolution by the molecular replacement method. The structure has been refined by restrained-parameter least-squares methods to a crystallographic R factor (= sigma parallel Fo magnitude of-Fo parallel/sigma magnitude of Fo) o of 0.198. CI-2 is a member of the potato inhibitor 1 family. It lacks the characteristic stabilizing disulfide bonds of most other members of serine proteinase inhibitor families. The body of CI-2 shows few conformational changes between the free inhibitor and the previously reported structure of CI-2 in complex with subtilisin Novo [McPhalen, C.A., Svendsen, I., Jonassen, I., & James, M.N.G. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7242-7246]. However, the reactive site loop has some significant conformational differences between the free inhibitor and its complexed form. The residues in this segment of polypeptide exhibit relatively large thermal motion parameters and some disorder in the uncomplexed form of the inhibitor. The reactive site bond is between Met-59I and Glu-60I in the consecutive sequential numbering of CI-2 (Met-60-Glu-61 according to the alignment of Svendsen et al. [Svendsen, I., Hejgaard, J., & Chavan, J.K. (1984) Carlsberg Res. Commun. 49, 493-502]). The network of hydrogen bonds and electrostatic interactions stabilizing the conformation of the reactive site loop is much less extensive in the free than in the complexed inhibitor.
About this Structure
2CI2 is a Single protein structure of sequence from Hordeum vulgare. This structure supersedes the now removed PDB entry 1CI2. Full crystallographic information is available from OCA.
Reference
Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds., McPhalen CA, James MN, Biochemistry. 1987 Jan 13;26(1):261-9. PMID:3828302
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