1jx5: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1jx5.png|left|200px]]
-<!--
+==THEORETICAL MODEL OF THE BETA-PROPELLER DOMAIN OF INTEGRIN ALPHAIIB==
-The line below this paragraph, containing "STRUCTURE_1jx5", creates the "Structure Box" on the page.
+<StructureSection load='1jx5' size='340' side='right'caption='[[1jx5]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JX5 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jx5 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1jx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jx5 ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1jx5|  PDB=1jx5  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Several distinct regions of the integrin alpha(IIb) subunit have been implicated in ligand binding. To localize the ligand binding sites in alpha(IIb), we swapped all 27 predicted loops with the corresponding sequences of alpha(4) or alpha(5). 19 of the 27 swapping mutations had no effect on binding to both fibrinogen and ligand-mimetic antibodies (e.g. LJ-CP3), suggesting that these regions do not contain major ligand binding sites. In contrast, swapping the remaining 8 predicted loops completely blocked ligand binding. Ala scanning mutagenesis of these critical predicted loops identified more than 30 discontinuous residues in repeats 2-4 and at the boundary between repeats 4 and 5 as critical for ligand binding. Interestingly, these residues are clustered in the predicted beta-propeller model, consistent with this model. Most of the critical residues are located at the edge of the upper face of the propeller, and several critical residues are located on the side of the propeller domain. None of the predicted loops in repeats 1, 6, and 7, and none of the four putative Ca(2+)-binding predicted loops on the lower surface of the beta-propeller were important for ligand binding. The results map an important ligand binding interface at the edge of the top and on the side of the beta-propeller toroid, centering on repeat 3.
-===THEORETICAL MODEL OF THE BETA-PROPELLER DOMAIN OF INTEGRIN ALPHAIIB===
+Amino acid residues in the alpha IIb subunit that are critical for ligand binding to integrin alpha IIbbeta 3 are clustered in the beta-propeller model.,Kamata T, Tieu KK, Irie A, Springer TA, Takada Y J Biol Chem. 2001 Nov 23;276(47):44275-83. Epub 2001 Sep 13. PMID:11557768<ref>PMID:11557768</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11557768}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1jx5" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11557768 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11557768}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JX5 OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:11557768</ref><references group="xtra"/>
 [[Category: Kamata, T]]
 [[Category: Springer, T A]]
 [[Category: Takada, Y]]
 [[Category: Tieu, K K]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 06:59:20 2010''