P53-DNA Recognition: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 21: | Line 21: | ||
Mutations of p53 residues are associated with 50% of human cancers. Such mutations are predominantly located in the p53-DNA binding domain (DBD) based on an analysis of human tumors (Figure 3). Particularly, arginine residues in the p53-DNA interface were found in tumors with high frequencies. | Mutations of p53 residues are associated with 50% of human cancers. Such mutations are predominantly located in the p53-DNA binding domain (DBD) based on an analysis of human tumors (Figure 3). Particularly, arginine residues in the p53-DNA interface were found in tumors with high frequencies. | ||
==Domain Architecture and Tetramerization | ==Structural Description of p53-DNA Complex== | ||
=Domain Architecture and Tetramerization= | |||
<Structure load='3kz8bio.pdb.zip' size='500' frame='true' align='right' caption='Figure 5: Crystal structure of p53 DBD tetramer-DNA complex, PDB ID 3KZ8.' scene='Sandbox_Reserved_170/Complex/6' /> | <Structure load='3kz8bio.pdb.zip' size='500' frame='true' align='right' caption='Figure 5: Crystal structure of p53 DBD tetramer-DNA complex, PDB ID 3KZ8.' scene='Sandbox_Reserved_170/Complex/6' /> | ||
| Line 31: | Line 33: | ||
The p53 DBD assumes the conformation of an <scene name='Sandbox_Reserved_170/Beta/1'>immunoglobulin-like fold consisting of a beta sandwich</scene>, which binds the response element in the major groove. A functionally important <scene name='Sandbox_Reserved_170/Zn/1'>Zn2+ ion coordinates the Cys176, His179, Cys238, Cys242 residues</scene> and, thus, stabilizes the fold of the DBD. | The p53 DBD assumes the conformation of an <scene name='Sandbox_Reserved_170/Beta/1'>immunoglobulin-like fold consisting of a beta sandwich</scene>, which binds the response element in the major groove. A functionally important <scene name='Sandbox_Reserved_170/Zn/1'>Zn2+ ion coordinates the Cys176, His179, Cys238, Cys242 residues</scene> and, thus, stabilizes the fold of the DBD. | ||
=Protein-Protein Interactions= | |||
<scene name='Sandbox_Reserved_170/Inter-dimer/4'> | The p53 tetramer forms a relatively small <scene name='Sandbox_Reserved_170/Intra-dimer/4'>intra-dimer with two salt bridges between Glu180 and Arg181 residues</scene> and a large <scene name='Sandbox_Reserved_170/Inter-dimer/4'>inter-dimer interface with an extensive network of interactions</scene>. | ||
<scene name='Sandbox_Reserved_170/Arg280_contact/5'>Arg280 contact</scene> | <scene name='Sandbox_Reserved_170/Arg280_contact/5'>Arg280 contact</scene> | ||
