Sandbox Reserved 1493: Difference between revisions

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The extracellular N-Terminus forms a cap over the β-propeller domain which is folded by seven successive blades of aminoterminal repeats. Each blade is a β-hairpin loop-like structure composed of 4 antiparallel β strands located in each repeat and connected by loops of the surface. This β-propeller is linked to a thigh and two calf domains, which form the leg structure that supports the heavy head. The total forms the stalk of the αIIb subunit. The region between the thigh and the first calf domain is the site at which the head region bends (in the inactivated form of the integrin) is called the knee of the subunit.

The β-propeller hosts multiple cation biding sites. The last 3 or 4 blades bind <scene name='80/802667/Ca_ions_on_beta-propeller/2'>Ca2+ ions</scene> which influence ligand binding on the lower side of the blades and plays an important role in biogenesis and stability of the heterodimer. The I domain inserted between blades 2 and 3 in the β-propeller follows a Rossman fold with five β-sheets surrounded by seven α-helices. Ligand binding occurs between the β-propeller and the β I domain of the β3 subunit via a coordinating Mg2+ ion in the MIDAS of the β3 subunit.

The β-propeller hosts multiple cation biding sites. The last 3 or 4 blades bind <scene name='80/802667/Ca_ions_on_beta-propeller/3'>Ca2+ ions</scene> which influence ligand binding on the lower side of the blades and plays an important role in biogenesis and stability of the heterodimer. The I domain inserted between blades 2 and 3 in the β-propeller follows a Rossman fold with five β-sheets surrounded by seven α-helices. Ligand binding occurs between the β-propeller and the β I domain of the β3 subunit via a coordinating Mg2+ ion in the MIDAS of the β3 subunit.

The RGD binding site (Arg-Gly-Asp) is in a crevice in this region, inserted between the β-propeller and β I domains. The Arg side chain is located in a groove on the upper surface of the propeller and the Asp carboxylate protruding into a cleft on the β I surface.

Sandbox Reserved 1493: Difference between revisions

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 The extracellular N-Terminus forms a cap over the β-propeller domain which is folded by seven successive blades of aminoterminal repeats. Each blade is a β-hairpin loop-like structure composed of 4 antiparallel β strands located in each repeat and connected by loops of the surface. This β-propeller is linked to a thigh and two calf domains, which form the leg structure that supports the heavy head. The total forms the stalk of the αIIb subunit. The region between the thigh and the first calf domain is the site at which the head region bends (in the inactivated form of the integrin) is called the knee of the subunit.
-The β-propeller hosts multiple cation biding sites. The last 3 or 4 blades bind <scene name='80/802667/Ca_ions_on_beta-propeller/2'>Ca2+ ions</scene> which influence ligand binding on the lower side of the blades and plays an important role in biogenesis and stability of the heterodimer. The I domain inserted between blades 2 and 3 in the β-propeller follows a Rossman fold with five β-sheets surrounded by seven α-helices. Ligand binding occurs between the β-propeller and the β I domain of the β3 subunit via a coordinating Mg2+ ion in the MIDAS of the β3 subunit.
+The β-propeller hosts multiple cation biding sites. The last 3 or 4 blades bind <scene name='80/802667/Ca_ions_on_beta-propeller/3'>Ca2+ ions</scene> which influence ligand binding on the lower side of the blades and plays an important role in biogenesis and stability of the heterodimer. The I domain inserted between blades 2 and 3 in the β-propeller follows a Rossman fold with five β-sheets surrounded by seven α-helices. Ligand binding occurs between the β-propeller and the β I domain of the β3 subunit via a coordinating Mg2+ ion in the MIDAS of the β3 subunit.
 The RGD binding site (Arg-Gly-Asp) is in a crevice in this region, inserted between the β-propeller and β I domains. The Arg side chain is located in a groove on the upper surface of the propeller and the Asp carboxylate protruding into a cleft on the β I surface.