User:Natalya Boufan/Sandbox 1
From Proteopedia
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The AceK structure contains two functional domains: a Kinase domain (KD) where the kinase, phosphatase and ATPase reactions occur, and a regulatory (RD) that helps form allosteric binding pockets involved in regulating the catalytic domain’s function. The <scene name='78/783138/Amp_binding/7'>AMP molecule</scene> is situated in a pocket at the interface between the KD and RD and acts as a bridge. | The AceK structure contains two functional domains: a Kinase domain (KD) where the kinase, phosphatase and ATPase reactions occur, and a regulatory (RD) that helps form allosteric binding pockets involved in regulating the catalytic domain’s function. The <scene name='78/783138/Amp_binding/7'>AMP molecule</scene> is situated in a pocket at the interface between the KD and RD and acts as a bridge. | ||
- | The <scene name='78/783138/Regulation_domain/4'>regulatory domain</scene>, which comprises the amino-terminal half of the AceK sequence, is mainly composed of a-helices. | + | The <scene name='78/783138/Regulation_domain/4'>regulatory domain</scene>, which comprises the amino-terminal half of the AceK sequence, is mainly composed of a-helices and hairpin structures.This domain represents a unique protein fold with no structural homologues. The regulatory domain is linked to the kinase domain by a 27-residue-long a-helix. The <scene name='78/783138/Kinase_domain/13'>kinase domain</scene>, which makes up the carboxy-terminal half of AceK, has a classic bi-lobe protein kinase fold with the <scene name='78/783138/Atp_binding_site/1'>ATP-binding cleft</scene> located at the interface between the two lobes. The N-terminal lobe consists mainly of a twisted, five-stranded, antiparallel b-sheet and two a-helices. The larger C-terminal lobe is predominantly a-helical with some stretches of antiparallel b-strands. The ATP molecule is under the cover of the five-stranded b-sheet and is shielded by <scene name='78/783138/Loopb/3'>loop-b3aC</scene>. Loop-b3aC shifts upwards or downwards to controls access to the ATP-binding site. The <scene name='78/783138/Srl/1'>substrate recognition loop</scene> (SRL) stretches out of the C-terminal lobe. This loop, together with loop-b3aC, forms a large cleft that is the <scene name='78/783138/Icdh_binding_cleft/1'>IDH binding site</scene>. |
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- | The <scene name='78/783138/Kinase_domain/13'>kinase domain</scene>, which makes up the carboxy-terminal half of AceK, has a classic bi-lobe protein kinase fold with the <scene name='78/783138/Atp_binding_site/1'>ATP-binding cleft</scene> located at the interface between the two lobes. The N-terminal lobe consists mainly of a twisted, five-stranded, antiparallel b-sheet and two a-helices. The larger C-terminal lobe is predominantly a-helical with some stretches of antiparallel b-strands. The ATP molecule is under the cover of the five-stranded b-sheet and is shielded by <scene name='78/783138/Loopb/3'>loop-b3aC</scene>. Loop-b3aC shifts upwards or downwards to controls access to the ATP-binding site. The <scene name='78/783138/Srl/1'>substrate recognition loop</scene> (SRL) stretches out of the C-terminal lobe. This loop, together with loop-b3aC, forms a large cleft that is the <scene name='78/783138/Icdh_binding_cleft/1'>IDH binding site</scene>. | + | |
= Function = | = Function = |
Revision as of 15:16, 19 March 2018
Isocitrate dehydrogenase kinase/phosphatase
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644