Sandbox122: Difference between revisions
From Proteopedia
Jump to navigationJump to search
David Bauché (talk | contribs) No edit summary |
David Bauché (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
STRUCTURE OF A FLAVIN-BINDING DOMAIN, LOV2, FROM THE CHIMERIC PHYTOCHROME/PHOTOTROPIN PHOTORECEPTOR PHY3 | |||
{{STRUCTURE_1g28| PDB=1g28 | SCENE= }} | {{STRUCTURE_1g28| PDB=1g28 | SCENE= }} | ||
'''Phototropin''' is a blue light receptor involved in the phototropism (it is a phenomenon which is growth directed by light).This is a transmembrane protein present on the top of coleoptile. | '''Phototropin''' is a blue light receptor involved in the phototropism (it is a phenomenon which is growth directed by light).This is a transmembrane protein present on the top of coleoptile. | ||
| Line 17: | Line 19: | ||
==Kinase regulation by LOV2== | ==Kinase regulation by LOV2== | ||
The current view of phototropin receptor activation is that LOV2 functions as a repressor of the C-terminal kinase domain in the dark and that this mode of repression is alleviated upon photoexcitation, resulting in receptor autophosphorylation.The predominant role of LOV2 in regulating phototropin activity appears to arise from its position within the phototropin molecule. Photoexcitation of an extended LOV2 fragment leads to displacement of an α-helix from the surface of the LOV2-core. | The current view of phototropin receptor activation is that LOV2 functions as a repressor of the C-terminal kinase domain in the dark and that this mode of repression is alleviated upon photoexcitation, resulting in receptor autophosphorylation.The predominant role of LOV2 in regulating phototropin activity appears to arise from its position within the phototropin molecule. Photoexcitation of an extended LOV2 fragment leads to displacement of an α-helix from the surface of the LOV2-core. | ||
== | ==Conclusion== | ||
Kinase will permit the autophosphorylation of phototropin. The rate of phosphorylatide phototropin acts to differential lateral gradients of auxin which is responsible of phototropism phenomenon. | Kinase will permit the autophosphorylation of phototropin. The rate of phosphorylatide phototropin acts to differential lateral gradients of auxin which is responsible of phototropism phenomenon. | ||
For more information about the continuation of this mechanism refer to this PDB protein: 2z6c,2z6d, | For more information about the continuation of this mechanism refer to this PDB protein: 2z6c,2z6d, | ||
==Reference and tools== | |||
John T. M. Kennis, Ivo H. M. van Stokkum, Sean Crosson, Magdalena Gauden, Keith Moffat, and Rienk van Grondelle:The LOV2 Domain of Phototropin: A Reversible Photochromic Switch.J. Am. Chem. Soc., 2004, 126 (14), pp 4512–4513 | |||
software used: pymol, chemstek | |||
==Proteopedia Page Contributors and editors== | |||
David Bauché | |||