2bkg: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2bkg.gif|left|200px]] | [[Image:2bkg.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN''' | {{Structure | ||
|PDB= 2bkg |SIZE=350|CAPTION= <scene name='initialview01'>2bkg</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2BKG is a [ | 2BKG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKG OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability., Binz HK, Kohl A, Pluckthun A, Grutter MG, Proteins. 2006 Nov 1;65(2):280-4. PMID:[http:// | Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability., Binz HK, Kohl A, Pluckthun A, Grutter MG, Proteins. 2006 Nov 1;65(2):280-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16493627 16493627] | ||
[[Category: ]] | [[Category: ]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: protein stability]] | [[Category: protein stability]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:03:05 2008'' | ||
Revision as of 14:03, 20 March 2008
| |||||||||||||
| 2bkg, resolution 1.90Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF E3_19 AN DESIGNED ANKYRIN REPEAT PROTEIN
Overview
Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very stable. The structural analysis of the designed AR protein E3_5 revealed that this stability is due to a regular fold with highly conserved structural motifs and H-bonding networks. However, the designed AR protein E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8 kcal/mol), despite 88% sequence identity. To investigate the structural correlations of this stability difference between E3_5 and E3_19, we determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as well has a regular AR domain fold with the characteristic H-bonding patterns. All structural features of the E3_5 and E3_19 molecules appear to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the two AR proteins. E3_19 features clusters of charged residues and more exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19 have been deposited in the Protein Data Bank. PDB ID: 2BKG.
About this Structure
2BKG is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Crystal structure of a consensus-designed ankyrin repeat protein: implications for stability., Binz HK, Kohl A, Pluckthun A, Grutter MG, Proteins. 2006 Nov 1;65(2):280-4. PMID:16493627 [[Category: ]]
Page seeded by OCA on Thu Mar 20 16:03:05 2008
