Cover Picture
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Cover Picture Lutz Schmitt and Robert Tampe ´ The cover picture shows a schematic representation of the recognition principle of the ABC transporter complex TAP, which was deciphered by using combinatorial peptide libraries. By comparing individual sublibraries with the complex library, the effect of each amino acid with respect to its position in the peptide sequence can be derived. Favored or disfavored residues are colored in blue and red, respectively. The decoded recognition pattern for antigenic peptides matched the binding motif of class I MHC molecules. Based on these experiments we now begin to understand how the transport and loading machinery TAP fulfills one of the most important tasks in cellular immune surveillance: constantly supplying antigenic peptides for subsequent presentation by class I MHC molecules to cytotoxic T lymphocytes. Further details are given in the review by L. Schmitt and R. Tampe ´ on p. 16 ff.
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Transcript of Cover Picture
Cover Picture
Lutz Schmitt and Robert TampeÂ
The cover picture shows a schematic representation of the recognition principle of theABC transporter complex TAP, which was deciphered by using combinatorial peptidelibraries. By comparing individual sublibraries with the complex library, the effect of eachamino acid with respect to its position in the peptide sequence can be derived. Favored ordisfavored residues are colored in blue and red, respectively. The decoded recognitionpattern for antigenic peptides matched the binding motif of class I MHC molecules. Basedon these experiments we now begin to understand how the transport and loadingmachinery TAP fulfills one of the most important tasks in cellular immune surveillance:constantly supplying antigenic peptides for subsequent presentation by class I MHCmolecules to cytotoxic T lymphocytes. Further details are given in the review by L. Schmittand R. Tampe on p. 16 ff.
6 � WILEY-VCH-Verlag GmbH, D-69451 Weinheim, 2000 1439-4227/00/01/01 $ 17.50+.50/0 CHEMBIOCHEM 2000, 1, No. 1
COVER PICTURE
The cover picture shows a schematic representation of the recognition principle of the ABCtransporter complex TAP, which was deciphered by using combinatorial peptide libraries. Bycomparing individual sublibraries with the complex library, the effect of each amino acid withrespect to its position in the peptide sequence can be derived. Favored or disfavored residues arecolored in blue and red, respectively. The decoded recognition pattern for antigenic peptidesmatched the binding motif of class I MHC molecules. Based on these experiments we now begin tounderstand how the transport and loading machinery TAP fulfills one of the most important tasksin cellular immune surveillance: constantly supplying antigenic peptides for subsequentpresentation by class I MHC molecules to cytotoxic T lymphocytes. Further details are given in thereview by L. Schmitt and R. Tampe on p. 16 ff.
REVIEW
In the defense mechanism against intracellular pathogensand tumors, the ABC transporter TAP plays an essential role. TheTAP complex mediates transport of antigenic peptides into theendoplasmic reticulum, where they are efficiently loaded ontomajor histocompatibility complex (MHC) class I molecules. Thepeptide ± MHC complexes are specifically recognized on the cellsurface by cytotoxic T lymphocytes, which eventually kill thecell. By applying combinatorial chemistry, a peptide-bindingmotif of TAP was established (see picture) from a library ofbillions of peptides.
L. Schmitt, R. TampeÂ*
16 ± 35
Affinity, Specificity, Diversity:A Challenge for the ABCTransporter TAP in CellularImmunity
HIGHLIGHT
Diabetes affects more than 142 million people worldwide ;however, little structural information is currently available forthe intact insulin receptor and its complex with the hormone.Recently, cryoelectron microscopy of the whole complex andX-ray crystallography of sections have been combined to tacklethe problem (see picture; � American Association for theAdvancement of Science, 1999). Here we review the latestapproaches in this direction.
U. Schell, M. Grün, R. Hilgenfeld *
37 ± 40
Binding of Insulin to ItsReceptor: Towards anUnderstanding in ThreeDimensions
FULL PAPERS
By disulfide interchange, dynamic combinatorial libraries(DCLs) can easily be generated from a range of carbohydratedimers. This mild and reversible redox interconversion betweendiscrete carbohydrate species also allows for in situ selection bya biologial receptor. In the present study, it is shown that theDCLs generated interact dynamically with the receptor, thelectin concanavalin A (see schematic picture), and that onespecies can be selected in favour of the other library compo-nents.
O. Ramström, J.-M. Lehn *
41 ± 48
In Situ Generation andScreening of a DynamicCombinatorial CarbohydrateLibrary against Concanavalin A
CHEMBIOCHEM 2000, 1, No. 1 � WILEY-VCH-Verlag GmbH, D-69451 Weinheim, 2000 1439-4227/00/01/01 $ 17.50+.50/0 7
Structure ± activity relationships can be used for studyingprotein transition states in the same way as for classicalchemical reactions, although protein folding transition statesare different from transition states in simple chemical reactionsbecause they involve the making and breaking of a largenumber of non-covalent interactions as the whole proteinstructure changes conformation. F-value analysis shows how afrequently used cosolvent perturbs the transition state of thetetramerisation domain of p53 (see picture) by inducingHammond-type behaviour. This has significant implications formechanistic studies on protein folding.
C.-P. B. Yiu, M. G. Mateu,A. R. Fersht *
49 ± 55
Protein Folding TransitionStates: Elicitation of HammondEffects by 2,2,2-Trifluoroethanol
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