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Structure paper

TitleThermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions.
Journal, issue, pagesACS MED. CHEM. LETT., Vol. 1, Page 448-452, Year 2010
Publish dateMay 27, 2010 (structure data deposition date)
AuthorsDelorbe, J.E. / Clements, J.H. / Whiddon, B.B. / Martin, S.F.
External linksACS MED. CHEM. LETT. / PubMed:21116482
MethodsX-ray diffraction
Resolution2 - 2.02 Å
Structure data

PDB-3n7y:
Crystal Structure of the Grb2 SH2 Domain in Complex with a 20-Membered Macrocyclic Ligand Having the Sequence pYVNV
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

PDB-3n84:
Crystal Structure of the Grb2 SH2 Domain in Complex with a 23-Membered Macrocyclic Ligand Having the Sequence pYVNVP
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3n8m:
Crystal Structure of the Grb2 SH2 Domain in Complex with An Acyclic Ligand Having the Sequence pYVNVP
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
Keywordsprotein binding/peptide / ligand preorganization / macrocycles / macrocyclic ligands / Golgi apparatus / Host-virus interaction / Phosphoprotein / protein binding-peptide complex / Grb2 SH2 domain

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