User:Wally Novak/Sandbox Hicks: Difference between revisions
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== Structural Highlights == | == Structural Highlights == | ||
<scene name='74/744126/Pcna_monomer_helixfront_2/1'> The PCNA monomers </scene> consist of 258 residues each and are a mass of 28.916 kDa. Each monomer contributes two domains to the trimeric ring. These domains possess anti-parallel beta sheets (blue) which approach each other on one end, but are separated by two alpha helices at the other (red), creating a 45 degree wedge in the sheets with alpha helices at the blunt end. The domains are connected by an extended beta sheet. This creates a <scene name='74/744126/6_fold_symmetry/1'> six-fold symmetry within the trimeric ring </scene> and it also creates a β-α-β-β-β motif going around the ring. <ref>8001157</ref> | <scene name='74/744126/Pcna_monomer_helixfront_2/1'> The PCNA monomers </scene> consist of 258 residues each and are a mass of 28.916 kDa. Each monomer contributes two domains to the trimeric ring. These domains possess anti-parallel beta sheets (blue) which approach each other on one end, but are separated by two alpha helices at the other (red), creating a 45 degree wedge in the sheets with alpha helices at the blunt end. The domains are connected by an extended beta sheet. This creates a <scene name='74/744126/6_fold_symmetry/1'> six-fold symmetry within the trimeric ring </scene> and it also creates a β-α-β-β-β motif going around the ring. <ref>PMID:8001157</ref> | ||
== Interaction with DNA == | == Interaction with DNA == | ||
Since PCNA is a sliding clamp protein, it must be able to loosely interact with DNA. | |||
<ref>doi:10.1006</ref> | |||
PCNA also has many <scene name='74/744126/Acidic_residues_pcna/1'>Text To Be Displayed</scene> | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:52, 11 October 2016
Proliferating Cell Nuclear Antigen
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