User:Karan Hingorani/sandbox 1
From Proteopedia
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===Structure=== | ===Structure=== | ||
| - | E.coli DHFR is a small 159 amino acid protein approximately 18kDa. It has an a/b structure with eight central B strands and four helices. The protein can be thought to be made up of two subdomains, divided by the active site cleft. The <scene name='User:Karan_Hingorani/sandbox_1/Adenosine_binding_loop/1'>Adenosine binding subdomain | + | E.coli DHFR is a small 159 amino acid protein approximately 18kDa. It has an a/b structure with eight central B strands and four helices. The protein can be thought to be made up of two subdomains, divided by the active site cleft. The <scene name='User:Karan_Hingorani/sandbox_1/Adenosine_binding_loop/1'>Adenosine binding subdomain which consists of residues 38-88 and the major subdomain comprised of about 100 residues. Three loops can be found in the major subdomain and they make up about 50% of this domain. They are the <scene name='User:Karan_Hingorani/sandbox_1/Met_20_loop/1'>Met20 loop</scene> (residues 9-24), the <scene name='User:Karan_Hingorani/sandbox_1/F-g_loop/1'>F-G loop</scene> (residues 116-132)and the <scene name='User:Karan_Hingorani/sandbox_1/G-h_loop/1'>G-H loop</scene> (residues 142-150). The Met20 loop assumes different conformations during catalysis and accomodation of ligands is made possible by the 'hinge bending' motion about Lys 38 and Val 88 of the Adenosine binding domain. |
Revision as of 21:07, 14 December 2011
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