User:Andrea Foote/Sandbox 1
From Proteopedia
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== Structure == | == Structure == | ||
| - | Purα functions as a dimer composed of two intramolecular domains and one intermolecular domain. The Purα monomer contains three semi-conserved repeated amino acid sequences, named in order from N->C: PUR repeats I, II, and III. These repeats fold to form two domains: <scene name='78/786627/5fgp_intro/8'>PUR repeats I and II</scene> associating to form the I-II domain or “intramolecular domain”, while <scene name='78/786627/5fgo_repeatiii/2'>PUR repeat III</scene> facilitates dimerization through association with a repeat III from a second Purα monomer or repeat III of Purβ. Each PUR repeat is connected by flexible linker regions. | ||
[[Image:180429 proteopedia pura figures2.jpg|thumb|right|300px| A PUR domain is analogous to a left-handed handshake. PUR repeat I-II represented from 5fgp.]] | [[Image:180429 proteopedia pura figures2.jpg|thumb|right|300px| A PUR domain is analogous to a left-handed handshake. PUR repeat I-II represented from 5fgp.]] | ||
| + | Purα is a Purα functions as a dimer composed of two intramolecular domains and one intermolecular domain. The Purα monomer contains three semi-conserved repeated amino acid sequences, named in order from N->C: PUR repeats I, II, and III. These repeats fold to form two domains: <scene name='78/786627/5fgp_intro/8'>PUR repeats I and II</scene> associating to form the I-II domain or “intramolecular domain”, while <scene name='78/786627/5fgo_repeatiii/2'>PUR repeat III</scene> facilitates dimerization through association with a repeat III from a second Purα monomer or repeat III of Purβ. Each PUR repeat is connected by flexible linker regions. Each PUR repeat contains a beta-sheet composed of four beta-strands, followed by a single alpha-helix. | ||
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| + | The domains of Purα have been described as "Whirly-like" folds because of their structural similarity to the DNA-binding Whirly class of proteins found in plants.<ref>PMID:19846792</ref> | ||
== Function == | == Function == | ||
High-affinity nucleic acid-binding function is dependent on Purα dimerization. Purα forms homodimers in addition to heterodimers with Purβ. PurA is known to repress various genes including | High-affinity nucleic acid-binding function is dependent on Purα dimerization. Purα forms homodimers in addition to heterodimers with Purβ. PurA is known to repress various genes including | ||
Revision as of 10:59, 3 May 2018
Purine-rich element binding protein alpha
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