1svx

From Proteopedia

(Difference between revisions)

Revision as of 11:35, 24 December 2020

Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein

Structural highlights

1svx is a 2 chain structure with sequence from [1] and "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1mj0
Gene:	MALE, B4034, Z5632, ECS5017 ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We report here the evolution of ankyrin repeat (AR) proteins in vitro for specific, high-affinity target binding. Using a consensus design strategy, we generated combinatorial libraries of AR proteins of varying repeat numbers with diversified binding surfaces. Libraries of two and three repeats, flanked by 'capping repeats,' were used in ribosome-display selections against maltose binding protein (MBP) and two eukaryotic kinases. We rapidly enriched target-specific binders with affinities in the low nanomolar range and determined the crystal structure of one of the selected AR proteins in complex with MBP at 2.3 A resolution. The interaction relies on the randomized positions of the designed AR protein and is comparable to natural, heterodimeric protein-protein interactions. Thus, our AR protein libraries are valuable sources for binding molecules and, because of the very favorable biophysical properties of the designed AR proteins, an attractive alternative to antibody libraries.

High-affinity binders selected from designed ankyrin repeat protein libraries.,Binz HK, Amstutz P, Kohl A, Stumpp MT, Briand C, Forrer P, Grutter MG, Pluckthun A Nat Biotechnol. 2004 May;22(5):575-82. Epub 2004 Apr 18. PMID:15097997^[1]

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

References

↑ Binz HK, Amstutz P, Kohl A, Stumpp MT, Briand C, Forrer P, Grutter MG, Pluckthun A. High-affinity binders selected from designed ankyrin repeat protein libraries. Nat Biotechnol. 2004 May;22(5):575-82. Epub 2004 Apr 18. PMID:15097997 doi:10.1038/nbt962

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1svx"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein==
-<StructureSection load='1svx' size='340' side='right' caption='[[1svx]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
+<StructureSection load='1svx' size='340' side='right'caption='[[1svx]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1svx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SVX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1svx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SVX FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mj0|1mj0]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mj0|1mj0]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MALE, B4034, Z5632, ECS5017 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1svx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svx OCA], [http://pdbe.org/1svx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1svx RCSB], [http://www.ebi.ac.uk/pdbsum/1svx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1svx ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1svx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svx OCA], [http://pdbe.org/1svx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1svx RCSB], [http://www.ebi.ac.uk/pdbsum/1svx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1svx ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Ankyrin|Ankyrin]]
+*[[Ankyrin 3D structures|Ankyrin 3D structures]]
-*[[Maltose-binding protein|Maltose-binding protein]]
+*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Amstutz, P]]
 [[Category: Binz, H K]]

1svx

From Proteopedia

Revision as of 11:35, 24 December 2020

Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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