1mm9

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[[Image:1mm9.gif|left|200px]]
 
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==Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD==
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The line below this paragraph, containing "STRUCTURE_1mm9", creates the "Structure Box" on the page.
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<StructureSection load='1mm9' size='340' side='right'caption='[[1mm9]], [[Resolution|resolution]] 1.66&Aring;' 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'>[[1mm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MM9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
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{{STRUCTURE_1mm9| PDB=1mm9 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm9 OCA], [https://pdbe.org/1mm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mm9 RCSB], [https://www.ebi.ac.uk/pdbsum/1mm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mm9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mm9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mm9 ConSurf].
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<div style="clear:both"></div>
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'''Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD'''
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==See Also==
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*[[Avidin 3D structures|Avidin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The RGD (arginine-glycine-aspartic acid) sequence is found in several important extracellular matrix proteins and serves as an adhesion ligand for members of the integrin family of cell-surface receptors. This sequence and flanking residues from fibronectin or osteopontin have been engineered into an accessible surface loop of streptavidin to create two new streptavidin variants (FN-SA or OPN-SA, respectively) that bind cells through the alpha(v)beta(3) and/or alpha(5)beta(1) integrin receptors. Their crystal structures confirm the design and construction of the mutants and provide evidence about the conformational dynamics of the RGD loops. The loops in the isomorphous crystal structures are involved in crystal-packing interactions and this stabilizes their structures. Even so, the loop in OPN-SA is slightly disordered and two of the residues are not seen in difference electron-density maps. Comparison with other experimentally determined structures of RGD loops in cell-adhesion molecules shows that these loops occupy a large subset of conformational space. This is consistent with the view that RGD loops, at least those involved in cell adhesion, sample a number of structures dynamically, a few of which display high affinity for appropriate receptors.
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[[Category: Large Structures]]
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==About this Structure==
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1MM9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM9 OCA].
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==Reference==
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Structural characterization and comparison of RGD cell-adhesion recognition sites engineered into streptavidin., Le Trong I, McDevitt TC, Nelson KE, Stayton PS, Stenkamp RE, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):828-34. Epub 2003, Apr 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12777798 12777798]
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[[Category: Single protein]]
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[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
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[[Category: McDevitt, T C.]]
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[[Category: Le Trong I]]
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[[Category: Nelson, K E.]]
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[[Category: McDevitt TC]]
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[[Category: Stayton, P S.]]
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[[Category: Nelson KE]]
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[[Category: Stenkamp, R E.]]
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[[Category: Stayton PS]]
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[[Category: Trong, I Le.]]
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[[Category: Stenkamp RE]]
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[[Category: Tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:24:46 2008''
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Current revision

Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD

PDB ID 1mm9

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