Molecular recognition in helix-loop-helix and helix-loop-helix-l eucine zipper domains. Design of repertoires and selection of high affinity ligands for natural proteins (Articolo in rivista)

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  • Molecular recognition in helix-loop-helix and helix-loop-helix-l eucine zipper domains. Design of repertoires and selection of high affinity ligands for natural proteins (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M211991200 (literal)
Alternative label
  • Ciarapica R., Rosati J., Cesareni G., Nasi S. (2003)
    Molecular recognition in helix-loop-helix and helix-loop-helix-l eucine zipper domains. Design of repertoires and selection of high affinity ligands for natural proteins
    in Journal of biological chemistry (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ciarapica R., Rosati J., Cesareni G., Nasi S. (literal)
Pagina inizio
  • 12182 (literal)
Pagina fine
  • 12190 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • We have isolated protein domains with the potential to interfere with the function of Id proteins, regulators of differentiation involved in angiogenesis and tumorigenesis. The paper is published in a valued international journal with an impact factor of 6.482. Classificazione SCImago, subject category Biochemistry: Q1 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 278 (literal)
Rivista
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  • R. Ciarapica dottoranda di ricerca (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • The paper presents an investigation of the molecular rules underlying specificity of recognition between macromolecular partners using phage display as an experimental tool. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biologia and Patologia Molecolari Consiglio Nazionale delle Ricerche, Università La Sapienza, 00185 Roma and Dipartimento di Biologia, Università Tor Vergata, 00133 Roma, Italy (literal)
Titolo
  • Molecular recognition in helix-loop-helix and helix-loop-helix-l eucine zipper domains. Design of repertoires and selection of high affinity ligands for natural proteins (literal)
Abstract
  • Helix-loop-helix (HLH) and helix-loop-helix-leucine zipper (HLHZip) are dimerization domains that mediate selective pairing among members of a large transcription factor family involved in cell fate determination. To investigate the molecular rules underlying recognition specificity and to isolate molecules interfering with cell proliferation and differentiation control, we assembled two molecular repertoires obtained by directed randomization of the binding surface in these two domains. For this strategy we selected the Heb HLH and Max Zip regions as molecular scaffolds for the randomization process and displayed the two resulting molecular repertoires on lambda phage capsids. By affinity selection, many domains were isolated that bound to the proteins Mad, Rox, MyoD, and Id2 with different levels of affinity. Although several residues along an extended surface within each domain appeared to contribute to dimerization, some key residues critically involved in molecular recognition could be identified. Furthermore, a number of charged residues appeared to act as switch points facilitating partner exchange. By successfully selecting ligands for four of four HLH or HLHZip proteins, we have shown that the repertoires assembled are rather general and possibly contain elements that bind with sufficient affinity to any natural HLH or HLHZip molecule. Thus they represent a valuable source of ligands that could be used as reagents for molecular dissection of functional regulatory pathways. (literal)
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