From Proteopedia
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| | {{STRUCTURE_1qab| PDB=1qab | SCENE= }} | | {{STRUCTURE_1qab| PDB=1qab | SCENE= }} |
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| - | '''The structure of human retinol binding protein with its carrier protein transthyretin reveals interaction with the carboxy terminus of RBP'''
| + | ===The structure of human retinol binding protein with its carrier protein transthyretin reveals interaction with the carboxy terminus of RBP=== |
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| - | ==Overview==
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| - | Whether ultimately utilized as retinoic acid, retinal, or retinol, vitamin A is transported to the target cells as all-trans-retinol bound to retinol-binding protein (RBP). Circulating in the plasma, RBP itself is bound to transthyretin (TTR, previously referred to as thyroxine-binding prealbumin). In vitro one tetramer of TTR can bind two molecules of retinol-binding protein. However, the concentration of RBP in the plasma is limiting, and the complex isolated from serum is composed of TTR and RBP in a 1 to 1 stoichiometry. We report here the crystallographic structure at 3.2 A of the protein-protein complex of human RBP and TTR. RBP binds at a 2-fold axis of symmetry in the TTR tetramer, and consequently the recognition site itself has 2-fold symmetry: Four TTR amino acids (Arg-21, Val-20, Leu-82, and Ile-84) are contributed by two monomers. Amino acids Trp-67, Phe-96, and Leu-63 and -97 from RBP are flanked by the symmetry-related side chains from TTR. In addition, the structure reveals an interaction of the carboxy terminus of RBP at the protein-protein recognition interface. This interaction, which involves Leu-182 and Leu-183 of RBP, is consistent with the observation that naturally occurring truncated forms of the protein are more readily cleared from plasma than full-length RBP. Complex formation prevents extensive loss of RBP through glomerular filtration, and the loss of Leu-182 and Leu-183 would result in a decreased affinity of RBP for TTR.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10052934}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10052934 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10052934}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Prealbumin]] | | [[Category: Prealbumin]] |
| | [[Category: Transthyretin]] | | [[Category: Transthyretin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:03:44 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:25:30 2008'' |
Revision as of 10:25, 27 July 2008
Template:STRUCTURE 1qab
The structure of human retinol binding protein with its carrier protein transthyretin reveals interaction with the carboxy terminus of RBP
Template:ABSTRACT PUBMED 10052934
About this Structure
Full crystallographic information is available from OCA.
Reference
The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP., Naylor HM, Newcomer ME, Biochemistry. 1999 Mar 2;38(9):2647-53. PMID:10052934
Page seeded by OCA on Sun Jul 27 13:25:30 2008
