Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action 1 1Edited by M. F. Summers

Almeida, Marcius S.; Cabral, Katia M. S.; Kurtenbach, Eleonora; Almeida, Fábio C. L.; Valente, Ana Paula

doi:10.1006/jmbi.2001.5252

Cited by 126 publications

(92 citation statements)

References 45 publications

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“…Tyr52, which is conserved in many Brassica SCRs (Supplementary information, Figure S3A), is sandwiched between the α-helix and the β-sheet (Supplementary information, Figure S3B), and this configuration may also contribute to the structural integrity of SCR9. Database searches revealed that the structure of SCR9 is similar to the structures of SCR8 [22], plant defensins [28], and scorpion neurotoxins [29] (Figure 3C), though the positions of their disulfides bonds are not conserved. Despite this high level of structural similarity, these proteins exhibit strikingly different surfaces (Supplementary information, Figure S3C), which may allow them to have different mechanisms of action and biological activities.…”

Section: The Structure Of Scr9mentioning

confidence: 97%

Structural basis for specific self-incompatibility response in Brassica

Han

et al. 2016

Cell Res

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Self-incompatibility (SI) is a widespread mechanism in flowering plants which prevents self-fertilization and inbreeding. In Brassica, recognition of the highly polymorphic S-locus cysteine-rich protein (SCR; or S-locus protein 11) by the similarly polymorphic S-locus receptor kinase (SRK) dictates the SI specificity. Here, we report the crystal structure of the extracellular domain of SRK9 (eSRK9) in complex with SCR9 from Brassica rapa. SCR9 binding induces eSRK9 homodimerization, forming a 2:2 eSRK:SCR heterotetramer with a shape like the letter "A". Specific recognition of SCR9 is mediated through three hyper-variable (hv) regions of eSRK9. Each SCR9 simultaneously interacts with hvI and one-half of hvII from one eSRK9 monomer and the other half of hvII from the second eSRK9 monomer, playing a major role in mediating SRK9 homodimerization without involving interaction between the two SCR9 molecules. Single mutations of residues critical for the eSRK9-SCR9 interaction disrupt their binding in vitro. Our study rationalizes a body of data on specific recognition of SCR by SRK and provides a structural template for understanding the co-evolution between SRK and SCR.

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Section: The Structure Of Scr9mentioning

confidence: 97%

Structural basis for specific self-incompatibility response in Brassica

Han

et al. 2016

Cell Res

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“…14,[16][17][18] In addition, a deficiency of hCAP-18/LL-37 in the skin of patients with atopic dermatitis may predestine an increased risk for skin infections. 19 In order to augment the local immune response with administration of HDP, we compared the topical administration of the synthetic peptide LL-37 to adenoviral delivery of the transgene for hCAP-18/LL-37. Transient cutaneous transgene expression may be a potential alternative to the application of synthetically derived proteins in the treatment of acute wounds.…”

Section: Introductionmentioning

confidence: 99%

Transient cutaneous adenoviral gene therapy with human host defense peptide hCAP-18/LL-37 is effective for the treatment of burn wound infections

et al. 2005

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“…The values for the amount of a-helix, b-sheet and non-ab structure for these proteins are given in the middle and bottom data sets of Table 2. The prediction for P. sativum plant defensin was compared both with homologous proteins and with real values from the NMR structure determined in our laboratory (Almeida et al, 2002). As can be seen (Table 2), the predicted values are in good agreement with the PDB data, taking in account the possible structural differences between the proteins used and their homologues.…”

Section: Resultsmentioning

confidence: 66%

Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics

2006

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With the advent of structural genomics, the need for fast structural information about unknown proteins has increased. We describe a new methodology, based on 13 C, 15 N and 1 H chemical shift dispersion to predict the amount of secondary structure of unassigned proteins from their 15 N-and/or 13 C-edited heteronuclear single quantum coherence (HSQC) spectra. This methodology has been coded into a software called PASSNMR (Prediction of the Amount of Secondary Structure by Nuclear Magnetic Resonance), which can be accessed directly from the Internet. PASSNMR program is a powerful tool for screening proteins for proteomic or structural genomic investigations when used with recent methodologies that take advantage of the use of the antibiotic rifampicin to selectively label the heterologous proteins expressed in E. coli. PASSNMR analysis can be useful as a first approach to predict the amount of secondary structure in proteins to structural genomics. Information about the secondary structure of proteins can be obtained even before protein purification, with small quantities of protein, just by performing two simple nuclear magnetic resonance (NMR) experiments and using PASSNMR program.

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Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action 1 1Edited by M. F. Summers

Cited by 126 publications

References 45 publications

Structural basis for specific self-incompatibility response in Brassica

Structural basis for specific self-incompatibility response in Brassica

Transient cutaneous adenoviral gene therapy with human host defense peptide hCAP-18/LL-37 is effective for the treatment of burn wound infections

Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics

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