1rl7

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1rl7.png|left|200px]]
 
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==MODEL STRUCTURE OF SP1 (STABLE PROTEIN 1) FROM ASPEN PLANT==
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The line below this paragraph, containing "STRUCTURE_1rl7", creates the "Structure Box" on the page.
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<StructureSection load='1rl7' size='340' side='right'caption='[[1rl7]]' 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=1RL7 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=1rl7 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1rl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rl7 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1rl7| PDB=1rl7 | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A three dimensional theoretical model of SP1 (stable protein 1), which is resistant to high temperature and biotic-stresses, is presented here. The model was generated by the application of homology modeling technique. The conformational rigidity imparted to the fold by the presence of hydrogen-bonded, C5, C7, C10 and C13 structures in the loop regions, multiple aromatic--aromatic interactions at the protein interior and on the surface, in addition to salt-links and hydrogen-bonds are primarily the major factors, responsible for the increased stability of protein. The putative protein family is characterized by motifs, E-x(0,1)-L-x-[AEGQS] and V-x(2,3)-L-x-[ADEGST] and the active site in the tertiary structure is formed by conserved aromatic and isoleucine clusters.
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===MODEL STRUCTURE OF SP1 (STABLE PROTEIN 1) FROM ASPEN PLANT===
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Structural features in the model of a thermostable and stress-resistant protein, SP1 from aspen.,Rathore RS, Narasimhamurthy T J Biomol Struct Dyn. 2004 Apr;21(5):651-5. PMID:14769057<ref>PMID:14769057</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_14769057}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1rl7" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14769057 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14769057}}
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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=1RL7 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:14769057</ref><references group="xtra"/>
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[[Category: Narasimhamurthy, T]]
[[Category: Narasimhamurthy, T]]
[[Category: Rathore, R S]]
[[Category: Rathore, R S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:38:50 2010''
 

Current revision

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

MODEL STRUCTURE OF SP1 (STABLE PROTEIN 1) FROM ASPEN PLANT

PDB ID 1rl7

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