Related ArticlesSolution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.
Proteins. 2005 May 1;59(2):347-55
Authors: le Maire A, Weber T, Saunier S, Broutin I, Antignac C, Ducruix A, Dardel F
Human nephrocystin is a protein associated with juvenile NPH, an autosomal recessive, inherited kidney disease responsible for chronic renal failure in children. It contains an SH3 domain involved in signaling pathways controlling cell adhesion and cytoskeleton organization. The solution structure of this domain was solved by triple resonance NMR spectroscopy. Within the core, the structure is similar to those previously reported for other SH3 domains but exhibits a number of specific noncanonical features within the polyproline ligand binding site. Some of the key conserved residues are missing, and the N-Src loop exhibits an unusual twisted geometry, which results in a narrowing of the binding groove. This is induced by the replacement of a conserved Asp, Asn, or Glu residue by a Pro at one side of the N-Src loop. A systematic survey of other SH3 domains also containing a Pro at this position reveals that most of them belong to proteins involved in cell adhesion or motility. A variant of this domain, which carries a point mutation causing NPH, was also analyzed. This change, L180P, although it corresponds to a nonconserved and solvent-exposed position, causes a complete loss of the tertiary structure. Similar effects are also observed with the L180A variant. This could be a context-dependent effect resulting from an interaction between neighboring charged side-chains.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
J Struct Funct Genomics. 2011 Jul 23;
Authors: Eletsky A, Ruyechan WT, Xiao R, Acton TB, Montelione GT, Szyperski T
The solution NMR structure of protein MED25(391-543), comprising the activator interacting domain (ACID) of subunit 25 of the human mediator, is presented along with the measurement of...
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[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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[NMR paper] NMR solution structure of the inserted domain of human leukocyte function associated
NMR solution structure of the inserted domain of human leukocyte function associated antigen-1.
Related Articles NMR solution structure of the inserted domain of human leukocyte function associated antigen-1.
J Mol Biol. 2000 Feb 4;295(5):1251-64
Authors: Legge GB, Kriwacki RW, Chung J, Hommel U, Ramage P, Case DA, Dyson HJ, Wright PE
The interaction between the leukocyte function-associated antigen-1 (LFA-1) and the intercellular adhesion molecule is thought to be mediated primarily via the inserted domain (I-domain) in the alpha-subunit. The...
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[NMR paper] NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin
NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Jan 14;275(2):1089-94
Authors: Huang W, Dolmer K, Liao X, Gettins PG
Human alpha(2)-macroglobulin-proteinase complexes bind to their receptor, the low density lipoprotein receptor-related protein (LRP), through a discrete 138-residue C-terminal receptor binding domain (RBD), which also binds to the beta-amyloid peptide. We have used NMR...
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[NMR paper] Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed muta
Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed mutagenesis.
Related Articles Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed mutagenesis.
Biochem J. 1999 Jul 15;341 ( Pt 2):355-61
Authors: Crocker PR, Vinson M, Kelm S, Drickamer K
The molecular interactions between sialoadhesin and sialylated ligands have been investigated by using proton NMR. Addition of ligands to the 12 kDa N-terminal immunoglobulin-like domain of sialoadhesin result in resonance shifts in the protein...
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[NMR paper] High-resolution solution NMR structure of the minimal active domain of the human immu
High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Related Articles High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Biochemistry. 1998 Dec 22;37(51):17704-13
Authors: Kodera Y, Sato K, Tsukahara T, Komatsu H, Maeda T, Kohno T
The retroviral nucleocapsid (NC) protein is a multifunctional protein essential for RNA genome packaging and viral infectivity. The NC protein, NCp8, of the...
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[NMR paper] NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotei
NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments.
Related Articles NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments.
Protein Eng. 1998 Oct;11(10):847-53
Authors: McAlister MS, Davis B, Pfuhl M, Driscoll PC
CD5 is a type-I transmembrane glycoprotein found on thymocytes, T-cells and a subset of B-cells. The extracellular region consists of three domains belonging to the...
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NMR structure of the human Mediator MED25 ACID domain.
NMR structure of the human Mediator MED25 ACID domain.
Related Articles NMR structure of the human Mediator MED25 ACID domain.
J Struct Biol. 2010 Oct 22;
Authors: Bontems F, Verger A, Dewitte F, Lens Z, Baert JL, Ferreira E, de Launoit Y, Sizun C, Guittet E, Villeret V, Monté D
MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts...
Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a muta
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