1ugl

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(New page: 200px<br /><applet load="1ugl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ugl" /> '''Solution structure of S8-SP11'''<br /> ==Ov...)
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[[Image:1ugl.jpg|left|200px]]<br /><applet load="1ugl" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of S8-SP11'''<br />
'''Solution structure of S8-SP11'''<br />
==Overview==
==Overview==
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Many flowering plants possess a self-incompatibility system to prevent, inbreeding. In Brassica rapa, self/non-self recognition in mating is, established through S-haplotype-specific interactions between stigma, receptors and S-locus protein 11 (SP11, also called S-locus cysteine-rich, protein) that is encoded at the highly polymorphic S-locus. Here we, describe the solution structure of the SP11 protein of the S8-haplotype, (S8-SP11), which specifically binds to the stigma factor of the same, haplotype. It folds into an alpha/beta sandwich structure that resembles, those of plant defensins. Residues important for structural integrity are, highly conserved among the allelic SP11s, suggesting the existence of a, common folding pattern. Structure-based sequence alignment and homology, modeling of allelic SP11 identified a hyper-variable (HV) region, which is, thought to form a loop that bulges out from the body of the protein that, is amenable to solvent exposure. We suggest that the HV region could serve, as a specific binding site for the stigma receptor.
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Many flowering plants possess a self-incompatibility system to prevent inbreeding. In Brassica rapa, self/non-self recognition in mating is established through S-haplotype-specific interactions between stigma receptors and S-locus protein 11 (SP11, also called S-locus cysteine-rich protein) that is encoded at the highly polymorphic S-locus. Here we describe the solution structure of the SP11 protein of the S8-haplotype (S8-SP11), which specifically binds to the stigma factor of the same haplotype. It folds into an alpha/beta sandwich structure that resembles those of plant defensins. Residues important for structural integrity are highly conserved among the allelic SP11s, suggesting the existence of a common folding pattern. Structure-based sequence alignment and homology modeling of allelic SP11 identified a hyper-variable (HV) region, which is thought to form a loop that bulges out from the body of the protein that is amenable to solvent exposure. We suggest that the HV region could serve as a specific binding site for the stigma receptor.
==About this Structure==
==About this Structure==
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1UGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UGL OCA].
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1UGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UGL OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Isogai, A.]]
[[Category: Isogai, A.]]
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[[Category: Jee, J.G.]]
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[[Category: Jee, J G.]]
[[Category: Kojima, C.]]
[[Category: Kojima, C.]]
[[Category: Mishima, M.]]
[[Category: Mishima, M.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Sasaki, K.]]
[[Category: Sasaki, K.]]
[[Category: Shirakawa, M.]]
[[Category: Shirakawa, M.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:58:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:15 2008''

Revision as of 13:24, 21 February 2008


1ugl

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Solution structure of S8-SP11

Overview

Many flowering plants possess a self-incompatibility system to prevent inbreeding. In Brassica rapa, self/non-self recognition in mating is established through S-haplotype-specific interactions between stigma receptors and S-locus protein 11 (SP11, also called S-locus cysteine-rich protein) that is encoded at the highly polymorphic S-locus. Here we describe the solution structure of the SP11 protein of the S8-haplotype (S8-SP11), which specifically binds to the stigma factor of the same haplotype. It folds into an alpha/beta sandwich structure that resembles those of plant defensins. Residues important for structural integrity are highly conserved among the allelic SP11s, suggesting the existence of a common folding pattern. Structure-based sequence alignment and homology modeling of allelic SP11 identified a hyper-variable (HV) region, which is thought to form a loop that bulges out from the body of the protein that is amenable to solvent exposure. We suggest that the HV region could serve as a specific binding site for the stigma receptor.

About this Structure

1UGL is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Structure of the male determinant factor for Brassica self-incompatibility., Mishima M, Takayama S, Sasaki K, Jee JG, Kojima C, Isogai A, Shirakawa M, J Biol Chem. 2003 Sep 19;278(38):36389-95. Epub 2003 Jun 30. PMID:12835321

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