1bus
From Proteopedia
(New page: 200px<br /><applet load="1bus" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bus" /> '''SOLUTION CONFORMATION OF PROTEINASE INHIBITO...) |
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'''SOLUTION CONFORMATION OF PROTEINASE INHIBITOR IIA FROM BULL SEMINAL PLASMA BY 1H NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY'''<br /> | '''SOLUTION CONFORMATION OF PROTEINASE INHIBITOR IIA FROM BULL SEMINAL PLASMA BY 1H NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A determination of the solution conformation of the proteinase inhibitor | + | A determination of the solution conformation of the proteinase inhibitor IIA from bull seminal plasma (BUSI IIA) is described. Two-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain a list of 202 distance constraints between individually assigned hydrogen atoms of the polypeptide chain, to identify the positions of the three disulfide bridges, and to locate the single cis peptide bond. Supplementary geometric constraints were derived from the vicinal spin-spin couplings and the locations of certain hydrogen bonds, as determined by nuclear magnetic resonance (n.m.r.). Using a new distance geometry program (DISGEO) which is capable of computing all-atom structures for proteins the size of BUSI IIA, five conformers were computed from the NOE distance constraints alone, and another five were computed with the supplementary constraints included. Comparison of the different structures computed from the n.m.r. data among themselves and with the crystal structures of two homologous proteins shows that the global features of the conformation of BUSI IIA (i.e. the overall dimensions of the molecule and the threading of the polypeptide chain) were well-defined by the available n.m.r. data. In the Appendix, we describe a preliminary energy refinement of the structure, which showed that the constraints derived from the n.m.r. data are compatible with a low energy spatial structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1BUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1BUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Guntert, P.]] | [[Category: Guntert, P.]] | ||
| - | [[Category: Havel, T | + | [[Category: Havel, T F.]] |
| - | [[Category: Williamson, M | + | [[Category: Williamson, M P.]] |
[[Category: Wuthrich, K.]] | [[Category: Wuthrich, K.]] | ||
[[Category: proteinase inhibitor]] | [[Category: proteinase inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:19 2008'' |
Revision as of 09:59, 21 February 2008
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SOLUTION CONFORMATION OF PROTEINASE INHIBITOR IIA FROM BULL SEMINAL PLASMA BY 1H NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY
Overview
A determination of the solution conformation of the proteinase inhibitor IIA from bull seminal plasma (BUSI IIA) is described. Two-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain a list of 202 distance constraints between individually assigned hydrogen atoms of the polypeptide chain, to identify the positions of the three disulfide bridges, and to locate the single cis peptide bond. Supplementary geometric constraints were derived from the vicinal spin-spin couplings and the locations of certain hydrogen bonds, as determined by nuclear magnetic resonance (n.m.r.). Using a new distance geometry program (DISGEO) which is capable of computing all-atom structures for proteins the size of BUSI IIA, five conformers were computed from the NOE distance constraints alone, and another five were computed with the supplementary constraints included. Comparison of the different structures computed from the n.m.r. data among themselves and with the crystal structures of two homologous proteins shows that the global features of the conformation of BUSI IIA (i.e. the overall dimensions of the molecule and the threading of the polypeptide chain) were well-defined by the available n.m.r. data. In the Appendix, we describe a preliminary energy refinement of the structure, which showed that the constraints derived from the n.m.r. data are compatible with a low energy spatial structure.
About this Structure
1BUS is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry., Williamson MP, Havel TF, Wuthrich K, J Mol Biol. 1985 Mar 20;182(2):295-315. PMID:3839023
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