Related ArticlesStructural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan.
Biochemistry. 2003 Nov 25;42(46):13717-24
Authors: Bozzi M, Bianchi M, Sciandra F, Paci M, Giardina B, Brancaccio A, Cicero DO
Dystroglycan (DG) is an adhesion molecule playing a crucial role for tissue stability during both early embriogenesis and adulthood and is composed by two tightly interacting subunits: alpha-DG, membrane-associated and highly glycosylated, and the transmembrane beta-DG. Recently, by solid-phase binding assays and NMR experiments, we have shown that the C-terminal domain of alpha-DG interacts with a recombinant extracellular fragment of beta-DG (positions 654-750) independently from glycosylation and that the linear binding epitope is located between residues 550 and 565 of alpha-DG. In order to elucidate which moieties of beta-DG are specifically involved in the complex with alpha-DG, the ectodomain has been recombinantly expressed and purified in a labeled ((13)C,(15)N) form and studied by multidimensional NMR. Although it represents a natively unfolded protein domain, we obtained an almost complete backbone assignment. Chemical shift index, (1)H-(15)N heteronuclear single-quantum coherence and nuclear Overhauser effect (HSQC-NOESY) spectra and (3)J(HN,H)(alpha) coupling constant values confirm that this protein is highly disordered, but (1)H-(15)N steady-state NOE experiments indicate that the protein presents two regions of different mobility. The first one, between residues 659 and 722, is characterized by a limited degree of mobility, whereas the C-terminal portion, containing about 30 amino acids, is highly flexible. The binding of beta-DG(654-750) to the C-terminal region of the alpha subunit, alpha-DG(485-620), has been investigated, showing that the region of beta-DG(654-750) between residues 691 and 719 is involved in the interaction.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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09-30-2011 06:00 AM
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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09-30-2011 05:59 AM
[NMR paper] NMR structure and peptide hormone binding site of the first extracellular domain of a
NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
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Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41
Authors: Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R
The corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands'...
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11-24-2010 10:01 PM
[NMR paper] NMR structural characterization of the N-terminal domain of the adenylyl cyclase-asso
NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.
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J Biomol NMR. 2004 May;29(1):73-84
Authors: Mavoungou C, Israel L, Rehm T, Ksiazek D, Krajewski M, Popowicz G, Noegel AA, Schleicher M, Holak TA
Cyclase-associated proteins (CAPs) are highly conserved, ubiquitous actin binding proteins that are involved in...
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11-24-2010 09:51 PM
[NMR paper] Structural analysis of the extracellular domain of vaccinia virus envelope protein, A
Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
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J Biol Chem. 2002 Jun 7;277(23):20949-59
Authors: Lin TH, Chia CM, Hsiao JC, Chang W, Ku CC, Hung SC, Tzou DL
This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa,...
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11-24-2010 08:49 PM
[NMR paper] NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobi
NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.
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Biochemistry. 2001 Mar 27;40(12):3561-71
Authors: Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ
Apomyoglobin forms a denatured state under low-salt conditions at pH 2.3. The conformational propensities and polypeptide backbone dynamics...
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11-19-2010 08:32 PM
NMR structure of the first extracellular domain of corticotropin releasing factor rec
NMR structure of the first extracellular domain of corticotropin releasing factor receptor 1 (ECD1-CRF-R1) complexed with a high affinity agonist.
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J Biol Chem. 2010 Sep 15;
Authors: Grace CR, Perrin MH, Gulyas J, Rivier JE, Vale WW, Riek R
The corticotropin releasing factor (CRF) peptide hormone family members coordinate endocrine, behavioral, autonomic and metabolic responses to...
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09-17-2010 04:14 PM
[NMR paper] NMR characterization of partially folded and unfolded conformational ensembles of pro
NMR characterization of partially folded and unfolded conformational ensembles of proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR characterization of partially folded and unfolded conformational ensembles of proteins.
Biopolymers. 1999;51(3):191-207
Authors: Barbar E
Studies of unfolded and partially folded proteins provide important insight into the initiation and process of protein folding. This review focuses on the...
Structural characterization by NMR of the natively unfolded extracellular domain of b
Linear Mode
