1X11
X11 PTB DOMAIN
Summary for 1X11
Entry DOI | 10.2210/pdb1x11/pdb |
Descriptor | X11, 13-MER PEPTIDE (3 entities in total) |
Functional Keywords | complex (peptide binding module-peptide), ptb domain, complex (peptide binding module-peptide) complex, complex (peptide binding module/peptide) |
Biological source | Homo sapiens (human) |
Cellular location | Membrane; Single-pass type I membrane protein: P05067 |
Total number of polymer chains | 4 |
Total formula weight | 42877.96 |
Authors | Lee, C.-H.,Zhang, Z.,Kuriyan, J. (deposition date: 1997-07-28, release date: 1998-01-14, Last modification date: 2024-11-13) |
Primary citation | Zhang, Z.,Lee, C.H.,Mandiyan, V.,Borg, J.P.,Margolis, B.,Schlessinger, J.,Kuriyan, J. Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. EMBO J., 16:6141-6150, 1997 Cited by PubMed Abstract: The crystal structure of the phosphotyrosine-binding domain (PTB) of the X11 protein has been determined, in complex with unphosphorylated peptides corresponding to a region of beta-amyloid precursor protein (betaAPP) that is required for receptor internalization. The mode of binding to X11 of the unphosphorylated peptides, which contain an NPxY motif, resembles that of phosphorylated peptides bound to the Shc and IRS-1 PTB domains. Eight peptide residues make specific contacts with the X11 PTB domain, and they collectively achieve high affinity (KD = 0.32 microM) and specificity. These results suggest that, in contrast to the SH2 domains, the PTB domains are primarily peptide-binding domains that have, in some cases, acquired specificity for phosphorylated tyrosines. PubMed: 9321393DOI: 10.1093/emboj/16.20.6141 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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