2lba: Difference between revisions

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-[[Image:2lba.png|left|200px]]
+==Solution structure of chicken ileal BABP in complex with glycochenodeoxycholic acid==
+<StructureSection load='2lba' size='340' side='right' caption='[[2lba]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+[[2lba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBA OCA]. <br>
+<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
+== Publication Abstract from PubMed ==
+Ileal bile acid binding proteins (I-BABP), belonging to the family of intracellular lipid binding proteins, control bile acid trafficking in enterocytes and participate in regulating the homeostasis of these cholesterol-derived metabolites. I-BABP orthologues share the same structural fold and are able to host up to two ligands in their large internal cavity. However variations in primary sequences determine differences in binding properties such as the degree of binding cooperativity. To investigate the molecular requirements for cooperativity we adopted a gain-of-function approach, exploring the possibility to turn the non-cooperative chicken I-BABP (cI-BABP) into a cooperative mutant protein. To this aim we first solved the solution structure of cI-BABP in complex with two molecules of the physiological ligand glycochenodeoxycholate. A comparative structural analysis with closely related members of the same protein family provided the basis to design a double mutant (H99Q/A101S cI-BABP) capable of establishing a cooperative binding mechanism. Molecular dynamics simulation studies of the wild type and mutant complexes and essential dynamics analysis of the trajectories supported the role of the identified amino acid residues as hot spot mediators of communication between binding sites. The emerging picture is consistent with a binding mechanism that can be described by an extended conformational selection model.
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+Structural requirements for cooperativity in ileal bile acid binding proteins.,Zanzoni S, Assfalg M, Giorgetti A, D'Onofrio M, Molinari H J Biol Chem. 2011 Sep 14. PMID:21917914<ref>PMID:21917914</ref>
-The line below this paragraph, containing "STRUCTURE_2lba", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2lba|  PDB=2lba  |  SCENE=  }}
-===Solution structure of chicken ileal BABP in complex with glycochenodeoxycholic acid===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+== References ==
+<references/>
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+__TOC__
-The line below this paragraph, {{ABSTRACT_PUBMED_21917914}}, adds the Publication Abstract to the page
+</StructureSection>
-(as it appears on PubMed at http://www.pubmed.gov), where 21917914 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_21917914}}
-==About this Structure==
-[[2lba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBA OCA].
-==Reference==
-<ref group="xtra">PMID:021917914</ref><references group="xtra"/>
 [[Category: Gallus gallus]]
 [[Category: Assfalg, M.]]