1rlb

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|PDB= 1rlb |SIZE=350|CAPTION= <scene name='initialview01'>1rlb</scene>, resolution 3.1&Aring;
|PDB= 1rlb |SIZE=350|CAPTION= <scene name='initialview01'>1rlb</scene>, resolution 3.1&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=REA:RETINOIC ACID'>REA</scene>
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|LIGAND= <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rlb OCA], [http://www.ebi.ac.uk/pdbsum/1rlb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rlb RCSB]</span>
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==Overview==
==Overview==
The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular interactions with the same transthyretin dimer, and each also made contacts with one of the other two monomers. Thus, the other two potential binding sites in a transthyretin tetramer were blocked. The amino acid residues of the retinol-binding protein that were involved in the contacts were close to the retinol-binding site.
The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular interactions with the same transthyretin dimer, and each also made contacts with one of the other two monomers. Thus, the other two potential binding sites in a transthyretin tetramer were blocked. The amino acid residues of the retinol-binding protein that were involved in the contacts were close to the retinol-binding site.
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==Disease==
 
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Known diseases associated with this structure: Amyloid neuropathy, familial, several allelic types OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]], Amyloidosis, senile systemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]], Carpal tunnel syndrome, familial OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]], Dystransthyretinemic hyperthyroxinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]], Retinol binding protein, deficiency of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=180250 180250]]
 
==About this Structure==
==About this Structure==
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[[Category: Monaco, H L.]]
[[Category: Monaco, H L.]]
[[Category: Rizzi, M.]]
[[Category: Rizzi, M.]]
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[[Category: REA]]
 
[[Category: complex (protein/protein)]]
[[Category: complex (protein/protein)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:29:44 2008''

Revision as of 20:29, 30 March 2008


PDB ID 1rlb

Drag the structure with the mouse to rotate
, resolution 3.1Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



RETINOL BINDING PROTEIN COMPLEXED WITH TRANSTHYRETIN


Overview

The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular interactions with the same transthyretin dimer, and each also made contacts with one of the other two monomers. Thus, the other two potential binding sites in a transthyretin tetramer were blocked. The amino acid residues of the retinol-binding protein that were involved in the contacts were close to the retinol-binding site.

About this Structure

1RLB is a Protein complex structure of sequences from Gallus gallus and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein., Monaco HL, Rizzi M, Coda A, Science. 1995 May 19;268(5213):1039-41. PMID:7754382

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