Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms.
|Abstract||PDZ domains most commonly bind the C-terminus of their protein targets. Typically the C-terminal four residues of the protein target are considered as the binding motif, particularly the C-terminal residue (P0) and third-last residue (P-2) that form the major contacts with the PDZ domain's "binding groove". We solved crystal structures of seven human PDZ domains, including five of the seven PDLIM family members. The structures of GRASP, PDLIM2, P ... [truncated at 450 characters in length]|
|Author||Elkins, Jonathan M; Gileadi, Carina; Shrestha, Leela; et al|
|Subject||Binding Sites Carrier Proteins Crystallography, X-Ray Humans Ligands Microfilament Proteins Models, Molecular PDZ Domains chemistry metabolism chemistry metabolism|
Structural impact of human and Escherichia coli biotin carboxyl carrier proteins on biotin attachment.
|Abstract||Holocarboxylase synthetase (HCS, human) and BirA (Escherichia coli) are biotin protein ligases that catalyze the ATP-dependent attachment of biotin to apocarboxylases. Biotin attachment occurs on a highly conserved lysine residue within a consensus sequence (Ala/Val-Met-Lys-Met) that is found in carboxylases in most organisms. Numerous studies have indicated that HCS and BirA, as well as biotin protein ligases from other organisms, can attach bio ... [truncated at 450 characters in length]|
|Author||Healy, Shannon; McDonald, Megan K; Wu, Xuchu; et al|
|Subject||Acetyl-CoA Carboxylase Carbon-Nitrogen Ligases Carrier Proteins Crystallography, X-Ray Escherichia coli Proteins Humans Methylmalonyl-CoA Decarboxylase Peptide Fragments Protein Binding Protein Structure, Tertiary Protein Subunits Repressor Proteins Substrate Specificity chemistry genetics metabolism chemistry genetics metabolism chemistry genetics metabolism chemistry genetics metabolism chemistry genetics metabolism chemistry metabolism genetics genetics chemistry genetics metabolism chemistry genetics metabolism genetics|
Thermolability of mutant MMACHC protein in the vitamin B12-responsive cblC disorder.
|Abstract||Methylmalonic aciduria and homocystinuria, cblC type, is the most common inborn error of cellular vitamin B12 metabolism. We previously showed that the protein carrying the mutation responsible for late-onset cblC (MMACHC-R161Q), treatable with high dose OHCbl, is able to bind OHCbl with wild-type affinity, leaving undetermined the disease mechanism involved [Froese et al., Mechanism of responsiveness, Mol. Genet. Metab. (2009).]. To assess wheth ... [truncated at 450 characters in length]|
|Author||Froese, D S; Healy, S; McDonald, M; et al|
|Subject||Age of Onset Amino Acid Metabolism, Inborn Errors Carrier Proteins Cobamides Fluorometry Homocystinuria Hot Temperature Humans Methylmalonic Acid Protein Denaturation Protein Stability Vitamin B 12 drug therapy genetics chemistry genetics chemistry drug therapy genetics urine analogs and derivatives chemistry genetics therapeutic use|