Reading between the lines: SH3 recognition of an intact protein.
The structure of Nef-SH3 domain complex reveals how an SH3 domain can more effectively 'read' its linear proline-rich recognition element when it is presented within the context of a folded protein.
Lim
W A
WA
Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
D001665:Binding Sites; D017124:Conserved Sequence / Q000235:genetics; D015693:Gene Products, nef / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011505:Protein-Tyrosine Kinases / Q000737:chemistry / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000378:metabolism; D051572:Proto-Oncogene Proteins c-hck; D018909:src Homology Domains / Q000235:genetics*
D015693:Gene Products, nef; D011518:Proto-Oncogene Proteins; D011505:Protein-Tyrosine Kinases; D051572:Proto-Oncogene Proteins c-hck