Sandbox Reserved 1097: Difference between revisions
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The 3D-structure at the top of the page represents the biological unit, it is the working part of the enzyme in in-vivo conditions but there is also a 3D-structure for the <scene name='82/829350/Asymmetric_unit/1'>asymmetric unit</scene> of TYRP1. | The 3D-structure at the top of the page represents the biological unit, it is the working part of the enzyme in in-vivo conditions but there is also a 3D-structure for the <scene name='82/829350/Asymmetric_unit/1'>asymmetric unit</scene> of TYRP1. | ||
TYRP1 is a globular monomeric protein. It is composed of several domains: a short peptide signal on the N-terminal side followed by a large intra-melanosomal domain. This intra-melanosomal domain contains a cystein-rich domain and a catalytic tyrosinase-like subdomain with two ion-binding sites.<ref name="Xlai">[Xuelei Lai, Harry J. Wichers, Montserrat Soler‐Lopez, Bauke W. Dijkstra. Structure and Function of Human Tyrosinase and Tyrosinase‐Related Proteins. 2018 Jan 2 Epub 2017 Nov 28 PMID: 29052256 https://www.ncbi.nlm.nih.gov/pubmed/29052256 DOI: 10.1002/chem.201704410 https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.201704410]</ref> The next part of the sequence is composed of a transmembrane α-helix followed by a short cytoplasmic sequence on the C-terminal chain.<ref name = "decker"> [Decker. H, Tuczek.F. The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One. 2017 Nov 13. Epub 2017 Oct 9 PMID: 28990327 https://www.ncbi.nlm.nih.gov/pubmed/28990327 DOI: 10.1002/anie.201708214 https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201708214]</ref> | TYRP1 is a globular monomeric protein. It is composed of several domains: a short peptide signal (0-25) on the N-terminal side followed by a large intra-melanosomal domain. This intra-melanosomal domain contains a cystein-rich domain and a catalytic tyrosinase-like subdomain with two ion-binding sites.<ref name="Xlai">[Xuelei Lai, Harry J. Wichers, Montserrat Soler‐Lopez, Bauke W. Dijkstra. Structure and Function of Human Tyrosinase and Tyrosinase‐Related Proteins. 2018 Jan 2 Epub 2017 Nov 28 PMID: 29052256 https://www.ncbi.nlm.nih.gov/pubmed/29052256 DOI: 10.1002/chem.201704410 https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.201704410]</ref> The next part of the sequence is composed of a transmembrane α-helix followed by a short cytoplasmic sequence on the C-terminal chain.<ref name = "decker"> [Decker. H, Tuczek.F. The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One. 2017 Nov 13. Epub 2017 Oct 9 PMID: 28990327 https://www.ncbi.nlm.nih.gov/pubmed/28990327 DOI: 10.1002/anie.201708214 https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201708214]</ref> | ||
* '''The cystein-rich subdomain''' ''(25-126)'' | * '''The cystein-rich subdomain''' ''(25-126)'' | ||
The cystein-rich domain has an epidermal growth factor‐like fold formed by two pairs of short antiparallel β-strands (62-66/98-102 and 116-118/124-126)<ref name= "lai"/> . This previous domain strongly interacts with the tyrosinase-like subdomain by the lastloop of the cystein-rich domain preceding the N-terminal domain. The role of the cystein-rich domain is still unknown, it is only found in [https://en.wikipedia.org/wiki/Mammal mammalians]. This domain is stabilized by three (42-65/56-99/101-110) disulfide bounds and is located at the opposite of the active site. It is said that the cystein-rich domain might help the formation of a complex between TYR and TYRP2.<ref name="Xlai"/><ref name= "lai"/> | The <scene name='82/829350/Domains/1'>cystein-rich domain</scene> has an epidermal growth factor‐like fold formed by two pairs of short antiparallel β-strands (62-66/98-102 and 116-118/124-126)<ref name= "lai"/> . This previous domain strongly interacts with the tyrosinase-like subdomain by the lastloop of the cystein-rich domain preceding the N-terminal domain. The role of the cystein-rich domain is still unknown, it is only found in [https://en.wikipedia.org/wiki/Mammal mammalians]. This domain is stabilized by three (42-65/56-99/101-110) disulfide bounds and is located at the opposite of the active site. It is said that the cystein-rich domain might help the formation of a complex between TYR and TYRP2.<ref name="Xlai"/><ref name= "lai"/> | ||
* '''The tyrosinase-like subdomain''' ''(127-477)'' | * '''The tyrosinase-like subdomain''' ''(127-477)'' | ||
