Mutations in Brca1 BRCT Domains

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 312: Line 312:
</jmolLink>
</jmolLink>
</jmol> between the two states. This mutation causes overpacking.
</jmol> between the two states. This mutation causes overpacking.
-
*'''Mutation L1764P:''' <scene name='75/752201/I1766s/1'>Wild type</scene> and the <jmol><jmolButton><script>frame next</script><text>Mutation</text></jmolButton></jmol>. This mutation probably decreased hydrophobic interaction.
+
*<scene name='75/752201/I1766s/1'>L1764S:</scene>
 +
<jmol>
 +
<jmolLink>
 +
<script>
 +
animation on; animation mode loop; frame 1 1 play; animation off; frame 1; select [LEU]1764;color selectionHalos green;selectionHalos on;
 +
</script>
 +
<text>Wild type </text>
 +
</jmolLink>
 +
</jmol>
 +
conformation and
 +
<jmol>
 +
<jmolLink>
 +
<script>
 +
animation on; animation mode loop; frame 2 2 play; animation off; frame 2; select [SER]1764;color selectionHalos red;selectionHalos on;
 +
</script>
 +
<text>mutation.
 +
</text>
 +
</jmolLink>
 +
</jmol>
 +
Click here to see the
 +
<jmol>
 +
<jmolLink>
 +
<script>
 +
animation off; frame all; select [SER]1764;color selectionHalos red;selectionHalos on;
 +
</script>
 +
<text>mutated and wild type
 +
</text>
 +
</jmolLink>
 +
</jmol> residues together, and an
 +
<jmol>
 +
<jmolLink>
 +
<script>
 +
animation on; animation mode loop; frame play; select [SER]1764;color selectionHalos red;selectionHalos on;
 +
</script>
 +
<text>animation
 +
</text>
 +
</jmolLink>
 +
</jmol> between the two states. This mutation probably decreased hydrophobic interaction.
*'''Mutation M1775R:''' <scene name='75/752201/M1775r/4'>Native hydrogen bonding interactions proximal to M1775</scene> ([[1t15]]) and <scene name='75/752201/M1775r/5'>hydrogen bonding, salt bridging for mutant M1775R. Arg-1775 participates in the coordination of two solvent
*'''Mutation M1775R:''' <scene name='75/752201/M1775r/4'>Native hydrogen bonding interactions proximal to M1775</scene> ([[1t15]]) and <scene name='75/752201/M1775r/5'>hydrogen bonding, salt bridging for mutant M1775R. Arg-1775 participates in the coordination of two solvent
anions, S1 and S2, and has been flipped out from the hydrophobic pocket where Met-1775 normally packs</scene> ([[1n5o]])<ref>PMID: 12427738</ref>. <scene name='75/752201/M1775r/6'>Mutated and wildtype residues together</scene>. <scene name='75/752201/M1775r/7'>Click here to see animation of this scene</scene>.
anions, S1 and S2, and has been flipped out from the hydrophobic pocket where Met-1775 normally packs</scene> ([[1n5o]])<ref>PMID: 12427738</ref>. <scene name='75/752201/M1775r/6'>Mutated and wildtype residues together</scene>. <scene name='75/752201/M1775r/7'>Click here to see animation of this scene</scene>.

Revision as of 10:16, 16 February 2017

Drag the structure with the mouse to rotate

References

  1. ↑ Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ. Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. Nat Struct Mol Biol. 2004 Jun;11(6):512-8. Epub 2004 May 9. PMID:15133502 doi:10.1038/nsmb775
  2. ↑ Williams RS, Glover JN. Structural consequences of a cancer-causing BRCA1-BRCT missense mutation. J Biol Chem. 2003 Jan 24;278(4):2630-5. Epub 2002 Nov 8. PMID:12427738 doi:10.1074/jbc.M210019200

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/Mutations_in_Brca1_BRCT_Domains"
Personal tools