Difference between revisions of "Part:BBa K5271000"
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| + | Figure 1. The 7D12 Binding Site on Domain III of sEGFR | ||
(A) Cartoon is shown with 7D12 colored green and sEGFRd3 colored gray. CDRs are highlighted in light green and labeled. (B) In this view, the structure has been rotated ∼180° about a vertical axis relative to (A). The expected locations of domains I, II, and IV of sEGFR are in light blue, based on the structure of tethered sEGFR in PDB ID 1NQL (Ferguson et al., 2003). (C) View of the interface region between 7D12 and sEGFRd3 in a similar orientation to (A). Side chains that participate in key interactions are shown as sticks, as is the sugar group on sEGFRd3. Predicted salt-bridge (≤4.5 Å) or hydrogen-bond (≤3.5 Å) interactions are indicated with dashed lines. Kabat numbering is used. | (A) Cartoon is shown with 7D12 colored green and sEGFRd3 colored gray. CDRs are highlighted in light green and labeled. (B) In this view, the structure has been rotated ∼180° about a vertical axis relative to (A). The expected locations of domains I, II, and IV of sEGFR are in light blue, based on the structure of tethered sEGFR in PDB ID 1NQL (Ferguson et al., 2003). (C) View of the interface region between 7D12 and sEGFRd3 in a similar orientation to (A). Side chains that participate in key interactions are shown as sticks, as is the sugar group on sEGFRd3. Predicted salt-bridge (≤4.5 Å) or hydrogen-bond (≤3.5 Å) interactions are indicated with dashed lines. Kabat numbering is used. | ||
Revision as of 08:10, 27 September 2024
EGFR-binding peptide
The EGFR binding peptide is a 124 amino acid long nanobody with a molecular weight of 13.4 kDa.
Usage and Biology
The epidermal growth factor receptor (EGFR) has been always found to be over-expressed in various type of drug-resistant human cancers, including pancreatic cancer and non-small cell lung cancer. It is a target of antibody-based chemotherapeutics for targeted immunotherapy. This EGFR binding peptide is a 124 amino acid long nanobody with an inhibitory effect on ligand-induced EGFR activation. It inhibits the EGFR activation by a steric blockade on the binding of ligands to EGFR. The EGFR binding peptide consists of the variable domains of heavy chain (VHH) only, which is the smallest antigen-binding modules occurs in the nature. The structure of the nanobody has been resolved using X-ray crystallography [Schmitz et al., 2013].
Figure 1. The 7D12 Binding Site on Domain III of sEGFR
(A) Cartoon is shown with 7D12 colored green and sEGFRd3 colored gray. CDRs are highlighted in light green and labeled. (B) In this view, the structure has been rotated ∼180° about a vertical axis relative to (A). The expected locations of domains I, II, and IV of sEGFR are in light blue, based on the structure of tethered sEGFR in PDB ID 1NQL (Ferguson et al., 2003). (C) View of the interface region between 7D12 and sEGFRd3 in a similar orientation to (A). Side chains that participate in key interactions are shown as sticks, as is the sugar group on sEGFRd3. Predicted salt-bridge (≤4.5 Å) or hydrogen-bond (≤3.5 Å) interactions are indicated with dashed lines. Kabat numbering is used. [Excerpt From Schmitz et al., 2013]
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 43
Illegal AgeI site found at 175 - 1000COMPATIBLE WITH RFC[1000]