1qab: Difference between revisions

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[[Image:1qab.gif|left|200px]]
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[[Image:1qab.png|left|200px]]


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{{STRUCTURE_1qab|  PDB=1qab  |  SCENE=  }}  
{{STRUCTURE_1qab|  PDB=1qab  |  SCENE=  }}  


'''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===




==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.
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{{ABSTRACT_PUBMED_10052934}}


==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

File:1qab.png

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

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