Sandbox 167: Difference between revisions

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Andrea Gorrell, James Jones

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 == Structure ==
-Composed of residues 868-1218, domain 3 (D3) also consists of a 20aa c domain, but said region was unable to be solved due to high disorder in the region. Composed of 7 α-helices and 16 β-strands, D3 is further organized into subdomains. The main portion of the enzyme appears to be a β-barrel structure composed of 10 antiparrallel strands connected via a Gly rich sequence to a 3 helix bundle. This bundle is stabilized by a hydrophobic core region as well as a multitude of H-bonding patterns. The β-barrel structure actually has some homology with the human muscle fatty acid binding protein (m-FABP, pdb= 1HMT). This, and other related proteins, form a "β-clam" subdomain structure for binding of hydrophobic molecules. However, other known β-clam structures do not possess enzymatic activity.
+Composed of residues 868-1218, domain 3 (D3) also consists of a 20aa C-terminal unresolved domain. Containing 7 α-helices and 16 β-strands, D3 is further organized into subdomains. The main portion of the enzyme appears to be a β-barrel structure composed of 10 anti-parallel strands connected via a Gly rich sequence to a 3 helix bundle. This bundle is stabilized by a hydrophobic core region as well as a multitude of H-bonding patterns<ref>PMID:15665092</ref>. The β-barrel structure actually has some homology with the human muscle fatty acid binding protein (m-FABP, pdb= 1HMT). This, and other related proteins, form a "β-clam" subdomain structure for binding of hydrophobic molecules. However, other known β-clam structures do not possess enzymatic activity<ref>PMID:15665092</ref>.
 Cropped Pymol image of 1vpr highlighting the β-barrel structure and tri-helix. The four histidine residues implied in pH-dependant activity regulation are highlighted in pink.