000005580 001__ 5580
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000005580 0248_ $$aoai:doc.rero.ch:20060403165755-RB$$ppostprint$$prero_explore$$zthesis_urn$$zreport$$zthesis$$zbook$$zjournal$$zcdu548$$zcdu16$$zpreprint$$zcdu1$$zdissertation$$zunine$$zcdu34
000005580 041__ $$aeng
000005580 080__ $$a548
000005580 100__ $$aLe Trong, Isolde$$uDepartments of Biological Structure and Biochemistry and the Biomolecular Structure Center, University of Washington, Seattle, USA
000005580 245__ $$9eng$$aCrystallographic Analysis of a Full-length Streptavidin with Its C-terminal Polypeptide Bound in the Biotin Binding Site
000005580 256__ $$apdf
000005580 269__ $$c2006-02-24
000005580 520__ $$9eng$$aThe structure of a full-length streptavidin has been determined at 1.7 Å resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150–153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin and peptidic ligands. The observed structure helps to rationalize the observations that full-length mature streptavidin binds biotinylated macromolecules with reduced affinity.
000005580 695__ $$9eng$$afull-length streptavidin ; crystallography ; self-binding ; protein/ligand interactions
000005580 700__ $$aHumbert, Nicolas$$uInstitut de Chimie, Université de Neuchâtel, Switzerland
000005580 700__ $$aWard, Thomas R.$$uInstitut de Chimie, Université de Neuchâtel, Switzerland
000005580 700__ $$aStenkamp, Ronald E.$$uDepartments of Biological Structure and Biochemistry and the Biomolecular Structure Center, University of Washington, Seattle, USA
000005580 773__ $$g2006/356/738-745$$tJournal of Molecular Biology
000005580 775__ $$gPublished Version$$ohttp://dx.doi.org/10.1016/j.jmb.2005.11.086
000005580 8564_ $$f1_Le_Trong_Isolde_-_Crystallographic_Analysis_of_a_Full-length_20060403.pdf$$qapplication/pdf$$s749687$$uhttp://doc.rero.ch/record/5580/files/1_Le_Trong_Isolde_-_Crystallographic_Analysis_of_a_Full-length_20060403.pdf$$yorder:1$$zTexte intégral
000005580 918__ $$aFaculté des sciences$$bRue Emile-Argand 11, 2007 Neuchâtel$$cInstitut de Chimie
000005580 919__ $$aUniversité de Neuchâtel$$bNeuchâtel$$ddoc.support@rero.ch
000005580 980__ $$aPOSTPRINT$$bUNINE
000005580 990__ $$a20060403165755-RB