1mm9

<StructureSection load='1mm9' size='340' side='right' caption='[[1mm9]], [[Resolution|resolution]] 1.66&Aring;' scene=''>

<table><tr><td colspan='2'>[[1mm9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MM9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1swe|1swe]], [[1mk5|1mk5]], [[1mep|1mep]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">core streptavidin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1895 AS 4.1583])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm9 OCA], [http://pdbe.org/1mm9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mm9 RCSB], [http://www.ebi.ac.uk/pdbsum/1mm9 PDBsum]</span></td></tr>

[[http://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).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mm9_consurf.spt"</scriptWhenChecked>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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:12777798<ref>PMID:12777798</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1mm9" style="background-color:#fffaf0;"></div>

*[[Avidin|Avidin]]

[[Category: As 4 1583]]

[[Category: McDevitt, T C]]

[[Category: Nelson, K E]]

[[Category: Stayton, P S]]

[[Category: Stenkamp, R E]]

[[Category: Trong, I Le]]

[[Category: Biotin-binding protein]]

[[Category: Tetramer]]