2roy: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2roy.gif|left|200px]] | [[Image:2roy.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2roy", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_2roy| PDB=2roy | SCENE= }} | |||
}} | |||
'''TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3',5'-DINITRO-N-ACETYL-L-THYRONINE''' | '''TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3',5'-DINITRO-N-ACETYL-L-THYRONINE''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2ROY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry | 2ROY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1roy 1roy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ROY OCA]. | ||
==Reference== | ==Reference== | ||
| Line 29: | Line 26: | ||
[[Category: Pangborn, W.]] | [[Category: Pangborn, W.]] | ||
[[Category: Wojtczak, A.]] | [[Category: Wojtczak, A.]] | ||
[[Category: | [[Category: Albumin]] | ||
[[Category: | [[Category: Amyloid]] | ||
[[Category: | [[Category: Cerebrospinal fluid]] | ||
[[Category: | [[Category: Disease mutation]] | ||
[[Category: | [[Category: Liver]] | ||
[[Category: | [[Category: Plasma]] | ||
[[Category: | [[Category: Polymorphism]] | ||
[[Category: | [[Category: Polyneuropathy]] | ||
[[Category: | [[Category: Prealbumin]] | ||
[[Category: | [[Category: Retinol-binding]] | ||
[[Category: | [[Category: Signal]] | ||
[[Category: | [[Category: Thyroid hormone]] | ||
[[Category: | [[Category: Thyroxine]] | ||
[[Category: | [[Category: Transport]] | ||
[[Category: | [[Category: Vitamin some]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:14:57 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:14, 4 May 2008
TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WITH 3',5'-DINITRO-N-ACETYL-L-THYRONINE
OverviewOverview
The molecular structures of two human transthyretin (hTTR, prealbumin) complexes, co-crystallized with thyroxine (3,5,3',5'-tetraiodo-L-thyronine; T(4)), and with 3',5'-dinitro-N-acetyl-LL-thyronine (DNNAT), were determined by X-ray diffraction methods. Crystals of both structures are orthorhombic, space group P2(1)2(1)2, and have two independent monomers in the asymmetric unit of the crystal lattice. These structures have been refined to 17.0% for 8-2.0 A resolution data for the T(4) complex (I), and to R = 18.4% for 8-2.2 A resolution data for the DNNAT structure (II). This report provides a detailed description of T(4) binding to wild-type hTTR at 2.0 A resolution, as well as DNNAT. In both structures, the two independent hormone-binding sites of the TTR tetramer are occupied by ligand. A 50% statistical disorder model was applied to account for the crystallographic twofold symmetry along the binding channel and the lack of such symmetry for the ligands. Results for the co-crystallized T(4) complex show that T(4) binds deep in the hormone-binding channel and displaces the bound water previously reported for T(4) soaked into a native transthyretin crystal [Blake & Oatley (1977). Nature (London), 268, 115-120]. DNNAT also binds deeper in the channel toward the tetramer center than T(4) with the nitro groups occupying the symmetrical innermost halogen pockets. The N-acetyl moiety does not form polar contacts with the protein side chains as it is oriented toward the center of the channel. The weak binding affinity of DNNAT results from the loss of hydrophobic interactions with the halogen binding pockets as observed in T(4) binding. These data suggest that the halogen-binding sites toward the tetramer center are of primary importance as they are occupied by analogues with weak affinity to TTR, and are therefore selected over the other halogen sites which contribute more strongly to the overall binding affinity.
About this StructureAbout this Structure
2ROY is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1roy. Full crystallographic information is available from OCA.
ReferenceReference
Structures of human transthyretin complexed with thyroxine at 2.0 A resolution and 3',5'-dinitro-N-acetyl-L-thyronine at 2.2 A resolution., Wojtczak A, Cody V, Luft JR, Pangborn W, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):758-65. PMID:15299640 Page seeded by OCA on Sun May 4 17:14:57 2008