1crb: Difference between revisions
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<StructureSection load='1crb' size='340' side='right' caption='[[1crb]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1crb' size='340' side='right' caption='[[1crb]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1crb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CRB FirstGlance]. <br> | <table><tr><td colspan='2'>[[1crb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CRB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=RTL:RETINOL'>RTL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=RTL:RETINOL'>RTL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1crb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1crb OCA], [http://pdbe.org/1crb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1crb RCSB], [http://www.ebi.ac.uk/pdbsum/1crb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1crb ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1crb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1crb OCA], [http://pdbe.org/1crb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1crb RCSB], [http://www.ebi.ac.uk/pdbsum/1crb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1crb ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1crb" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1crb" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Black rat]] | |||
[[Category: Cowan, S W]] | [[Category: Cowan, S W]] | ||
[[Category: Jones, T A]] | [[Category: Jones, T A]] | ||
[[Category: Cellular lipophilic transport protein]] | [[Category: Cellular lipophilic transport protein]] | ||
Revision as of 09:29, 29 November 2017
CRYSTALLOGRAPHIC STUDIES ON A FAMILY OF CELLULAR LIPOPHILIC TRANSPORT PROTEINS. REFINEMENT OF P2 MYELIN PROTEIN AND THE STRUCTURE DETERMINATION AND REFINEMENT OF CELLULAR RETINOL-BINDING PROTEIN IN COMPLEX WITH ALL-TRANS-RETINOLCRYSTALLOGRAPHIC STUDIES ON A FAMILY OF CELLULAR LIPOPHILIC TRANSPORT PROTEINS. REFINEMENT OF P2 MYELIN PROTEIN AND THE STRUCTURE DETERMINATION AND REFINEMENT OF CELLULAR RETINOL-BINDING PROTEIN IN COMPLEX WITH ALL-TRANS-RETINOL
Structural highlights
Function[RET1_RAT] Intracellular transport of retinol. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedP2 myelin protein (P2) and cellular retinol binding protein (CRBP) are members of a family of cellular lipophilic transport proteins. P2 has been refined at a resolution of 2.7 A, and CRBP has been solved by molecular replacement and refined to a resolution of 2.1 A. The members of this family form a compact three-dimensional structure built up from ten antiparallel strands that fold to form an orthogonal barrel containing the ligand. In P2, the carboxylate group of an oleic acid ligand interacts with the side-chains of two arginine (106 and 126), and one tyrosine (128) residues. The ligand adopts a U-shaped conformation. In CRBP, the all-trans-retinol has a planar conformation with its alcohol group hydrogen bonding to the side-chain of glutamine 108 (equivalent to residue 106 in P2). The local interactions of glutamine 108 explain CRBP's preference for binding retinol rather than retinal. The side-chain of lysine 40 makes a close contact with the isoprene tail of the retinol. Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol.,Cowan SW, Newcomer ME, Jones TA J Mol Biol. 1993 Apr 20;230(4):1225-46. PMID:7683727[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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