1d5u: Difference between revisions
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==MOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN F== | |||
<StructureSection load='1d5u' size='340' side='right' caption='[[1d5u]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D5U FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d5u FirstGlance], [http://www.ebi.ac.uk/pdbsum/1d5u PDBsum]</span></td></tr> | |||
<table> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Brandt, W]] | [[Category: Brandt, W]] | ||
[[Category: Bromme, D]] | [[Category: Bromme, D]] | ||
[[Category: Fengler, A]] | [[Category: Fengler, A]] | ||
[[Category: Mehler, E]] | [[Category: Mehler, E]] | ||
Revision as of 09:50, 4 September 2014
MOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN FMOLECULAR MODEL OF THE MATURE HUMAN CATHEPSIN F
Structural highlights
Publication Abstract from PubMedModels 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 |
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