From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:1cbi.jpg|left|200px]] | + | {{Seed}} |
| + | [[Image:1cbi.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1cbi| PDB=1cbi | SCENE= }} | | {{STRUCTURE_1cbi| PDB=1cbi | SCENE= }} |
| | | |
- | '''APO-CELLULAR RETINOIC ACID BINDING PROTEIN I'''
| + | ===APO-CELLULAR RETINOIC ACID BINDING PROTEIN I=== |
| | | |
| | | |
- | ==Overview==
| + | <!-- |
- | A recombinant form of murine apo-cellular retinoic acid binding protein I (apo-CRABPI) has been purified and crystallized at pH 5.0, and the crystal structure has been refined to an R-factor of 19.6% at a resolution of 2.7 A. CRABPI binds all-trans retinoic acid and some retinoic acid metabolites with nanomolar affinities. Coordinates of the holo form of CRABP were not available during the early stages of the study, and in spite of numerous homologs of known structure, phases were not obtainable through molecular replacement. Instead, an interpretable electron density map was obtained by multiple isomorphous replacement methods after improvement of the heavy-atom parameters with density modified trial phases. Two molecules of apo-CRABPI occupy the P3121 asymmetric unit and are related by pseudo 2-fold rotational symmetry. Unique conformational differences are apparent between the two molecules. In all of the family members studied to date, there is a lack of hydrogen bonds between two of the component beta-strands resulting in a gap in the interstand hydrogen bonding pattern. In the crystallographic dimer described here, a continuous intermolecular beta-sheet is formed by using this gap region. This is possible because of an 8 A outward maximum displacement of the tight turn between the third and fourth beta-strands on one of the molecules. The result is a double beta-barrel containing two apo-CRABPI molecules with a more open, ligand-accessible binding cavity, which has not been observed in other structures of a family of proteins that bind hydrophobic ligands.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7563063}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 7563063 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_7563063}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 26: |
Line 30: |
| [[Category: Thompson, J R.]] | | [[Category: Thompson, J R.]] |
| [[Category: Retinoic-acid transport]] | | [[Category: Retinoic-acid transport]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:33:12 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:30:52 2008'' |
Revision as of 17:30, 30 June 2008
Template:STRUCTURE 1cbi
APO-CELLULAR RETINOIC ACID BINDING PROTEIN I
Template:ABSTRACT PUBMED 7563063
About this Structure
1CBI is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet., Thompson JR, Bratt JM, Banaszak LJ, J Mol Biol. 1995 Sep 29;252(4):433-46. PMID:7563063
Page seeded by OCA on Mon Jun 30 20:30:52 2008