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| - | [[Image:1uij.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1uij.png|left|200px]] |
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| | {{STRUCTURE_1uij| PDB=1uij | SCENE= }} | | {{STRUCTURE_1uij| PDB=1uij | SCENE= }} |
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| - | '''Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)'''
| + | ===Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)=== |
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| - | ==Overview==
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| - | beta-Conglycinin is composed of three kinds of subunit: alpha, alpha' and beta. A phagocytosis-stimulating peptide sequence (MITLAIPVNKPGR), soymetide, exists in the alpha' subunit of beta-conglycinin. Met at N terminus of the soymetide is essential for the activity. When Thr at the third residue from N terminus of the soymetide is replaced by Phe or Trp, the phagocytosis-stimulating activity greatly increases (Thr<Phe<Trp). The beta subunit does not exhibit the phagocytosis-stimulating activity because the residues corresponding to the first and third residues in the soymetide are Ile and Lys, respectively. In this study, we introduced the phagocytosis-stimulating peptide sequence (Ile-->Met, Lys-->Thr, Phe, or Trp) into the beta subunit after confirmation of the effects of residue replacements by molecular modeling, suggesting that the introduced mutations might not prevent the correct folding. The studies of circular dichroism (CD), gel filtration and differential scanning calorimetry (DSC) of the mutants (I122M/K124T, I122M/K124F, I122M/K124W) expressed in E. coli demonstrated that they folded and self-assembled similarly to the wild type. This was confirmed by X-ray analysis of I122M/K124W crystal where the biggest residue tryptophane was introduced. The three mutants exhibited phagocytosis activities after digestion by trypsin, and the order was the wild type<I122M/K124T<I122M/K124F<I122M/K124W as expected.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12758152}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12758152 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12758152}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Double-stranded beta helix]] | | [[Category: Double-stranded beta helix]] |
| | [[Category: Seed storage protein]] | | [[Category: Seed storage protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:16:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:29:25 2008'' |
Revision as of 11:29, 29 July 2008
Template:STRUCTURE 1uij
Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)
Template:ABSTRACT PUBMED 12758152
About this Structure
1UIJ is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity., Maruyama N, Maruyama Y, Tsuruki T, Okuda E, Yoshikawa M, Utsumi S, Biochim Biophys Acta. 2003 May 30;1648(1-2):99-104. PMID:12758152
Page seeded by OCA on Tue Jul 29 14:29:25 2008
