1kja

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1kja.png|left|200px]]
 
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==THEORETICAL MODEL OF E-SELECTIN, C-TYPE LECTIN DOMAIN, RESIDUES 1-120, CELL ADHESION MOLECULE==
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The line below this paragraph, containing "STRUCTURE_1kja", creates the "Structure Box" on the page.
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<StructureSection load='1kja' size='340' side='right'caption='[[1kja]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KJA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1kja FirstGlance], [https://www.ebi.ac.uk/pdbsum/1kja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kja ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1kja| PDB=1kja | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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E- and P-selectin are cell adhesion molecules implicated in the early events of inflammation. Three-dimensional models of the lectin domains have been reported by us and others prior to the availability of X-ray structural information. The models have been used to outline the ligand binding site in the selectins and to identify residues critical for function. Recently, the crystal structure of E-selectin has been reported, and thus, comparison of our E-selectin model with the X-ray data is now possible. The comparison shows that the assumptions on which the modeling was based were generally correct and provides an instructive example for the opportunities and the limitations of comparative modeling.
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===THEORETICAL MODEL OF E-SELECTIN, C-TYPE LECTIN DOMAIN, RESIDUES 1-120, CELL ADHESION MOLECULE===
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Comparison of a protein model with its X-ray structure: the ligand binding domain of E-selectin.,Bajorath J, Stenkamp R, Aruffo A Bioconjug Chem. 1995 Jan-Feb;6(1):3-6. PMID:7536042<ref>PMID:7536042</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_7536042}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1kja" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 7536042 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_7536042}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJA OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:7536042</ref><references group="xtra"/>
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[[Category: Aruffo, A]]
[[Category: Aruffo, A]]
[[Category: Bajorath, J]]
[[Category: Bajorath, J]]
[[Category: Stenkamp, R]]
[[Category: Stenkamp, R]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 09:01:36 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THEORETICAL MODEL OF E-SELECTIN, C-TYPE LECTIN DOMAIN, RESIDUES 1-120, CELL ADHESION MOLECULE

PDB ID 1kja

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