About: A Heterospecific Leucine Zipper Tetramer

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	A Heterospecific Leucine Zipper Tetramer
Creator	Liu, Jie Deng, Yiqun Li, Qunnu Lu, Min Zheng, Qi Kallenbach, Neville
source	Elsevier; Medline; PMC
abstract	Protein-protein interactions dictate the assembly of the macromolecular complexes essential for functional networks and cellular behavior. Elucidating principles of molecular recognition governing important interfaces such as coiled coils is a challenging goal for structural and systems biology. We report here that two valine-containing mutants of the GCN4 leucine zipper that fold individually as four-stranded coiled coils associate preferentially in mixtures to form an antiparallel, heterotetrameric structure. X-ray crystallographic analysis reveals that the coinciding hydrophobic interfaces of the hetero- and homotetramers differ in detail, explaining their partnering and structural specificity. Equilibrium disulfide exchange and thermal denaturation experiments show that the 50-fold preference for heterospecificity results from a combination of preferential packing and hydrophobicity. The extent of preference is sensitive to the side chains comprising the interface. Thus, heterotypic versus homotypic interaction specificity in coiled coils reflects a delicate balance in complementarity of shape and chemistry of the participating side chains.
has issue date	2008-09-22(xsd:dateTime)
bibo:doi	10.1016/j.chembiol.2008.07.008
bibo:pmid	18804028
has license	no-cc
sha1sum (hex)	c615f013fb4574e31dc9034028e178cb88c2e49b
schema:url	https://doi.org/10.1016/j.chembiol.2008.07.008
resource representing a document's title	A Heterospecific Leucine Zipper Tetramer
has PubMed Central identifier	PMC7111190
has PubMed identifier	18804028
schema:publication	Chem Biol
resource representing a document's body	covid:c615f013fb4574e31dc9034028e178cb88c2e49b#body_text
is schema:about of	named entity 'exchange' named entity 'side chains' named entity 'specificity' named entity 'coils' named entity 'Tetramer' named entity 'LEUCINE ZIPPER' named entity 'COMPLEXES' named entity 'SHAPE' named entity 'SPECIFICITY' named entity 'COMBINATION' named entity 'CHAINS' named entity 'STRUCTURE' named entity 'REPORT' named entity 'COILED' named entity 'BALANCE' named entity 'INTERFACE' named entity 'CONTAINING' named entity 'THERMAL' named entity 'GCN4' named entity 'ARTICLE' named entity 'RESULTS' named entity 'NETWORKS' named entity 'REFLECTS' named entity 'GOAL' named entity 'STRUCTURAL' named entity 'LEUCINE ZIPPER' named entity 'PREFERENCE' named entity 'THEIR' named entity 'MUTANTS' named entity 'FOLD' named entity 'IMPORTANT' named entity 'EQUILIBRIUM' named entity 'FUNCTIONAL' named entity 'DENATURATION' named entity 'SENSITIVE TO' named entity 'TO FORM' named entity 'EXPERIMENTS' named entity 'BEHAVIOR' named entity 'VALINE' named entity 'SYSTEMS BIOLOGY' named entity 'MOLECULAR RECOGNITION' named entity 'HYDROPHOBIC' named entity 'DISULFIDE' named entity 'X-RAY CRYSTALLOGRAPHIC ANALYSIS' named entity 'ASSEMBLY' named entity 'EXTENT OF' named entity 'HERE' named entity 'ESSENTIAL' named entity 'IS A' named entity 'INTERACTION' named entity 'PACKING' named entity 'REVEALS' named entity 'EXCHANGE' named entity 'MIXTURES' named entity 'COMPLEMENTARITY' named entity 'ASSOCIATE' named entity 'HYDROPHOBICITY' named entity 'CHEMISTRY' named entity 'PARTICIPATING' named entity 'CELLULAR' named entity 'COILS' named entity 'PROTEIN-PROTEIN INTERACTIONS' covid:arg/c615f013fb4574e31dc9034028e178cb88c2e49b named entity 'molecular recognition' named entity 'disulfide' named entity 'zipper' named entity 'shape' named entity 'dictate' named entity 'delicate' named entity 'systems biology' named entity 'molecular recognition' named entity 'Protein-protein interactions' named entity 'Leucine Zipper' named entity 'mutants' named entity 'homotetramers' named entity 'hydrophobic'

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