Sandbox Reserved 1493: Difference between revisions

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=== KQAGDV binding site ===

On stimulated platelets, αIIbβ3 has a highly specific receptor for the plasma protein '''fibrinogen'''. The '''KQAGDV binding site''' interacts with the <scene name='80/802667/Fibrinogen_gamma_c_from_2vdo/1'>fibrinogen γ-chain C~~</scene>~~ terminus at the γHHLGGAKQAGDV sequence (residues 400 to 411 of γC). KQAGD is the minimal binding motif for αIIbβ3. The Asp side chain interacts with <scene name='80/802667/Mg_in_beta_head_midas/1'>Mg2+</scene> (MIDAS) and the Gly residue enters in a pocket between the two subunits. The peptide of the ligand extends on a large active site on the integrin and has a turn in the backbone that leads the Lys side chain of the KQAGdV sequence into a pocket, so that its ammonium group is involved in hydrogen bonding with the αIIb subunit.

On stimulated platelets, αIIbβ3 has a highly specific receptor for the plasma protein '''fibrinogen'''. The '''KQAGDV binding site''' interacts with the <scene name='80/802667/Fibrinogen_gamma_c_from_2vdo/2'>fibrinogen γ-chain C terminus at the γHHLGGAKQAGDV sequence</scene> (residues 400 to 411 of γC). <scene name='80/802667/Fibrinogen_gamma_c_kqagd/1'>KQAGD</scene> is the minimal binding motif for αIIbβ3. The Asp side chain interacts with <scene name='80/802667/Mg_in_beta_head_midas/1'>Mg2+</scene> (MIDAS) and the Gly residue enters in a pocket between the two subunits. The peptide of the ligand extends on a large active site on the integrin and has a turn in the backbone that leads the Lys side chain of the KQAGdV sequence into a pocket, so that its ammonium group is involved in hydrogen bonding with the αIIb subunit.

=== RGD binding site ===

Sandbox Reserved 1493: Difference between revisions

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@@ Line 61: / Line 61: @@
 === KQAGDV binding site ===
-On stimulated platelets, αIIbβ3 has a highly specific receptor for the plasma protein '''fibrinogen'''. The '''KQAGDV binding site''' interacts with the <scene name='80/802667/Fibrinogen_gamma_c_from_2vdo/1'>fibrinogen γ-chain C</scene> terminus at the γHHLGGAKQAGDV sequence (residues 400 to 411 of γC). KQAGD is the minimal binding motif for αIIbβ3. The Asp side chain interacts with <scene name='80/802667/Mg_in_beta_head_midas/1'>Mg2+</scene> (MIDAS) and the Gly residue enters in a pocket between the two subunits. The peptide of the ligand extends on a large active site on the integrin and has a turn in the backbone that leads the Lys side chain of the KQAGdV sequence into a pocket, so that its ammonium group is involved in hydrogen bonding with the αIIb subunit.
+On stimulated platelets, αIIbβ3 has a highly specific receptor for the plasma protein '''fibrinogen'''. The '''KQAGDV binding site''' interacts with the <scene name='80/802667/Fibrinogen_gamma_c_from_2vdo/2'>fibrinogen γ-chain C terminus at the γHHLGGAKQAGDV sequence</scene> (residues 400 to 411 of γC). <scene name='80/802667/Fibrinogen_gamma_c_kqagd/1'>KQAGD</scene> is the minimal binding motif for αIIbβ3. The Asp side chain interacts with <scene name='80/802667/Mg_in_beta_head_midas/1'>Mg2+</scene> (MIDAS) and the Gly residue enters in a pocket between the two subunits. The peptide of the ligand extends on a large active site on the integrin and has a turn in the backbone that leads the Lys side chain of the KQAGdV sequence into a pocket, so that its ammonium group is involved in hydrogen bonding with the αIIb subunit.
 === RGD binding site ===