1d5u: Difference between revisions

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1d5u.png|left|200px]]


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==MOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN F==
The line below this paragraph, containing "STRUCTURE_1d5u", creates the "Structure Box" on the page.
<StructureSection load='1d5u' size='340' side='right'caption='[[1d5u]]' 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=1D5U FirstGlance]. <br>
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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=1d5u FirstGlance], [https://www.ebi.ac.uk/pdbsum/1d5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d5u ProSAT]</span></td></tr>
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</table>
{{STRUCTURE_1d5u|  PDB=1d5u  |  SCENE= }}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Models of the tertiary structures of cathepsins K, S, H, and F were constructed by using homology protein modelling methods and refinements by interactive graphics and energy minimisation. The predicted structures yield information regarding their substrate binding sites and indicate the residues surrounding these sites. The ligand binding sites were characterised and compared with each other by means of calculated molecular electrostatic surface potentials. This will allow designing and development of new ligands specific for these cathepsins in future investigations.


===MOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN F===
Development and validation of homology models of human cathepsins K, S, H, and F.,Fengler A, Brandt W Adv Exp Med Biol. 2000;477:255-60. PMID:10849752<ref>PMID:10849752</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
{{ABSTRACT_PUBMED_10849752}}
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</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5U OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:10849752</ref><references group="xtra"/>
[[Category: Brandt, W]]
[[Category: Brandt, W]]
[[Category: Bromme, D]]
[[Category: Bromme, D]]
[[Category: Fengler, A]]
[[Category: Fengler, A]]
[[Category: Mehler, E]]
[[Category: Mehler, E]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 09:34:46 2010''

Latest revision as of 13:43, 14 July 2021

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

MOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN FMOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN F

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

Models of the tertiary structures of cathepsins K, S, H, and F were constructed by using homology protein modelling methods and refinements by interactive graphics and energy minimisation. The predicted structures yield information regarding their substrate binding sites and indicate the residues surrounding these sites. The ligand binding sites were characterised and compared with each other by means of calculated molecular electrostatic surface potentials. This will allow designing and development of new ligands specific for these cathepsins in future investigations.

Development and validation of homology models of human cathepsins K, S, H, and F.,Fengler A, Brandt W Adv Exp Med Biol. 2000;477:255-60. PMID:10849752[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Fengler A, Brandt W. Development and validation of homology models of human cathepsins K, S, H, and F. Adv Exp Med Biol. 2000;477:255-60. PMID:10849752
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