Atkinson A

References (2)

Title : Insights into a highly conserved network of hydrogen bonds in the agonist binding site of nicotinic acetylcholine receptors: A structural and theoretical study - Atkinson_2014_Proteins_82_2303
Author(s) : Atkinson A , Graton J , Le Questel JY
Ref : Proteins , 82 :2303 , 2014
Abstract : Structural and theoretical studies on the geometrical features of a hydrogen-bond network occurring in the binding site of nicotinic acetylcholine receptors (nAChRs) and composed of interconnected WxPD (Trp-x-Pro-Asp) and SWyz (Ser-Trp-yz) sequences from loops A and B, respectively, have been carried out. Multiple sequence alignments using as template the sequence of the apoform of Aplysia californica acetylcholine binding protein (Ac-AChBP) show the strict conservation of serine and tryptophan residues of the loop B SWyz sequence. Considering a sample of 19 high resolution AChBP structures, the strong conformational preferences of the key tryptophan residue has been pointing out, whatever the form, free or bounded, of AChBP. The geometry of the motif hydrogen-bond network has been characterized through the analyses of seven distances. The robustness of the various hydrogen-bond interactions is pointed out, the one involving the aspartate carboxylate group and the serine residue being the shortest of the network. The role of a cooperative effect involving a NH(His145)...OH (Ser142) hydrogen bond is highlighted. Density functional theory calculations on several simplified models based on the motif hydrogen-bond network allow probing the importance of the various hydrogen-bond interactions. The removal of the Ser142 hydroxyl group induces strong structural rearrangements, in agreement with the structural observations. Molecular electrostatic potential calculations on model systems highlight the importance of a cooperative effect in the whole hydrogen-bond network. More precisely, the key role of the Ser142 hydroxyl group, involved in several hydrogen bonds, is underlined. Proteins 2014; 82:2303-2317. (c) 2014 Wiley Periodicals, Inc.
ESTHER : Atkinson_2014_Proteins_82_2303
PubMedSearch : Atkinson_2014_Proteins_82_2303
PubMedID: 24752960

Title : The DNA sequence and biological annotation of human chromosome 1 - Gregory_2006_Nature_441_315
Author(s) : Gregory SG , Barlow KF , McLay KE , Kaul R , Swarbreck D , Dunham A , Scott CE , Howe KL , Woodfine K , Spencer CC , Jones MC , Gillson C , Searle S , Zhou Y , Kokocinski F , McDonald L , Evans R , Phillips K , Atkinson A , Cooper R , Jones C , Hall RE , Andrews TD , Lloyd C , Ainscough R , Almeida JP , Ambrose KD , Anderson F , Andrew RW , Ashwell RI , Aubin K , Babbage AK , Bagguley CL , Bailey J , Beasley H , Bethel G , Bird CP , Bray-Allen S , Brown JY , Brown AJ , Buckley D , Burton J , Bye J , Carder C , Chapman JC , Clark SY , Clarke G , Clee C , Cobley V , Collier RE , Corby N , Coville GJ , Davies J , Deadman R , Dunn M , Earthrowl M , Ellington AG , Errington H , Frankish A , Frankland J , French L , Garner P , Garnett J , Gay L , Ghori MR , Gibson R , Gilby LM , Gillett W , Glithero RJ , Grafham DV , Griffiths C , Griffiths-Jones S , Grocock R , Hammond S , Harrison ES , Hart E , Haugen E , Heath PD , Holmes S , Holt K , Howden PJ , Hunt AR , Hunt SE , Hunter G , Isherwood J , James R , Johnson C , Johnson D , Joy A , Kay M , Kershaw JK , Kibukawa M , Kimberley AM , King A , Knights AJ , Lad H , Laird G , Lawlor S , Leongamornlert DA , Lloyd DM , Loveland J , Lovell J , Lush MJ , Lyne R , Martin S , Mashreghi-Mohammadi M , Matthews L , Matthews NS , Mclaren S , Milne S , Mistry S , Moore MJ , Nickerson T , O'Dell CN , Oliver K , Palmeiri A , Palmer SA , Parker A , Patel D , Pearce AV , Peck AI , Pelan S , Phelps K , Phillimore BJ , Plumb R , Rajan J , Raymond C , Rouse G , Saenphimmachak C , Sehra HK , Sheridan E , Shownkeen R , Sims S , Skuce CD , Smith M , Steward C , Subramanian S , Sycamore N , Tracey A , Tromans A , Van Helmond Z , Wall M , Wallis JM , White S , Whitehead SL , Wilkinson JE , Willey DL , Williams H , Wilming L , Wray PW , Wu Z , Coulson A , Vaudin M , Sulston JE , Durbin R , Hubbard T , Wooster R , Dunham I , Carter NP , McVean G , Ross MT , Harrow J , Olson MV , Beck S , Rogers J , Bentley DR , Banerjee R , Bryant SP , Burford DC , Burrill WD , Clegg SM , Dhami P , Dovey O , Faulkner LM , Gribble SM , Langford CF , Pandian RD , Porter KM , Prigmore E
Ref : Nature , 441 :315 , 2006
Abstract : The reference sequence for each human chromosome provides the framework for understanding genome function, variation and evolution. Here we report the finished sequence and biological annotation of human chromosome 1. Chromosome 1 is gene-dense, with 3,141 genes and 991 pseudogenes, and many coding sequences overlap. Rearrangements and mutations of chromosome 1 are prevalent in cancer and many other diseases. Patterns of sequence variation reveal signals of recent selection in specific genes that may contribute to human fitness, and also in regions where no function is evident. Fine-scale recombination occurs in hotspots of varying intensity along the sequence, and is enriched near genes. These and other studies of human biology and disease encoded within chromosome 1 are made possible with the highly accurate annotated sequence, as part of the completed set of chromosome sequences that comprise the reference human genome.
ESTHER : Gregory_2006_Nature_441_315
PubMedSearch : Gregory_2006_Nature_441_315
PubMedID: 16710414
Gene_locus related to this paper: human-LYPLAL1 , human-PPT1 , human-TMCO4 , human-TMEM53