Macromolecular NMR spectroscopy for the non‐spectroscopist

Kwan, Ann H.; Mobli, Mehdi; Gooley, Paul R.; King, Glenn F.; Mackay, Joel P.

doi:10.1111/j.1742-4658.2011.08004.x

Cited by 153 publications

(146 citation statements)

References 68 publications

(90 reference statements)

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“…34 A, respectively, for the backbone of the full sequence range 1-83) (Figs 3B and 5 and Table 1), they can both be considered qualitatively as 'low resolution' [51]. Upon exclusion of the first two N-terminal residues (unstructured and not presenting long range NOEs), the resolution is A) and for the conformational functional epitope [26,44] formed by residues 60-83 (A/B 0.51/0.58 A).…”

Section: A Noncanonical Disulfide Bonding Pattern In Bitistatin Bmentioning

confidence: 99%

NMRstructure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins

et al. 2014

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Extant disintegrins, as found in the venoms of Viperidae and Crotalidae snakes (vipers and rattlesnakes, represent a family of polypeptides that block the function of b1 and b3 integrin receptors, both potently and with a high degree of selectivity. This toxin family owes its origin to the neofunctionalization of the extracellular region of an ADAM (a disintegrin and metalloprotease) molecule recruited into the snake venom gland proteome in the Jurassic. The evolutionary structural diversification of the disintegrin scaffold, from the ancestral long disintegrins to the more recently evolved medium-sized, dimeric and short disintegrins, involved the stepwise loss of pairs of class-specific disulfide linkages and the processing of the N-terminal region. NMR and crystal structures of medium-sized, dimeric and short disintegrins have been solved. However, the structure of a long disintegrin remained unknown. The present study reports the NMR solution structures of two disulfide bond conformers of the long disintegrin bitistatin from the African puff adder Bitis arietans. The findings provide insight into how a structural domain of the extracellular region of an ADAM molecule, recruited into and selectively expressed in the snake venom gland proteome as a PIII metalloprotease in the Jurassic, has subsequently been tranformed into a family of integrin receptor antagonists.

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Section: A Noncanonical Disulfide Bonding Pattern In Bitistatin Bmentioning

confidence: 99%

NMRstructure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins

et al. 2014

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“…Together these parameters indicate that the solution structure of Lmo2 LIM2 -Ldb1 LID is of medium to high resolution. 24 The structure of this tethered complex closely resembles that of other LIM-Ldb1 LID complexes, 22,23,[25][26][27] [e.g. Fig.…”

Section: Resultsmentioning

confidence: 93%

Solution structure of a tethered Lmo2_LIM2/Ldb1_LID complex

Dastmalchi¹,

Wilkinson-White²,

Kwan³

et al. 2012

Protein Science

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LIM-only protein 2, Lmo2, is a regulatory protein that is essential for hematopoietic development and inappropriate overexpression of Lmo2 in T-cells contributes to T-cell leukemia. It exerts its functions by mediating protein-protein interactions and nucleating multicomponent transcriptional complexes. Lmo2 interacts with LIM domain binding protein 1 (Ldb1) through the tandem LIM domains of Lmo2 and the LIM interaction domain (LID) of Ldb1. Here, we present the solution structure of the LIM2 domain of Lmo2 bound to Ldb1 LID . The ordered regions of Ldb1 in this complex correspond well with binding hotspots previously defined by mutagenic studies. Comparisons of this Lmo2 LIM2 -Ldb1 LID structure with previously determined structures of the Lmo2/Ldb1 LID complexes lead to the conclusion that modular binding of tandem LIM domains in Lmo2 to tandem linear motifs in Ldb1 is accompanied by several disorder-to-order transitions and/ or conformational changes in both proteins.

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“…Other than those for tryptophan side chains ( 15 N, ϳ130 ppm; 1 H, ϳ10 ppm), the only non-GST peaks that are visible for these proteins are poorly dispersed and lie in the "unfolded" regions of the spectra (Fig. 5, C and D) (63), suggesting that these constructs are not well folded and are probably molten globule-like. On the whole, these data indicate that Ldb1 LID and Isl1 LBD can form specific interactions with the LIM domains of Isl1, but the negative control LBDs, Switched and Scrambled, do not.…”

Section: Generation Of Tethered Complexes and Negative Controlmentioning

confidence: 96%

A Structural Basis for the Regulation of the LIM-Homeodomain Protein Islet 1 (Isl1) by Intra- and Intermolecular Interactions

Gadd¹,

Jacques²,

Nisevic³

et al. 2013

Journal of Biological Chemistry

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Background: A putative intramolecular interaction in the Islet 1 (Isl1) transcription factor inhibits DNA binding. Results: An intramolecular interaction between the LIM domains and LIM homeobox 3 (Lhx3)-binding domain in Isl1 was characterized. Conclusion:The intramolecular interaction within Isl1 is weak but specific. Significance: This interaction likely prevents unproductive binding in the absence of cofactor proteins.

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Macromolecular NMR spectroscopy for the non‐spectroscopist

Cited by 153 publications

References 68 publications

NMRstructure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins

NMRstructure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins

Solution structure of a tethered Lmo2_LIM2/Ldb1_LID complex

A Structural Basis for the Regulation of the LIM-Homeodomain Protein Islet 1 (Isl1) by Intra- and Intermolecular Interactions

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Macromolecular NMR spectroscopy for the non‐spectroscopist

Cited by 153 publications

References 68 publications

NMRstructure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins

NMRstructure of bitistatin – a missing piece in the evolutionary pathway of snake venom disintegrins

Solution structure of a tethered Lmo2LIM2/Ldb1LID complex

A Structural Basis for the Regulation of the LIM-Homeodomain Protein Islet 1 (Isl1) by Intra- and Intermolecular Interactions

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Solution structure of a tethered Lmo2_LIM2/Ldb1_LID complex