1abz
From Proteopedia
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|PDB= 1abz |SIZE=350|CAPTION= <scene name='initialview01'>1abz</scene> | |PDB= 1abz |SIZE=350|CAPTION= <scene name='initialview01'>1abz</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1abz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abz OCA], [http://www.ebi.ac.uk/pdbsum/1abz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1abz RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Fezoui, Y.]] | [[Category: Fezoui, Y.]] | ||
[[Category: Osterhout, J J.]] | [[Category: Osterhout, J J.]] | ||
| - | [[Category: NH2]] | ||
[[Category: de novo design]] | [[Category: de novo design]] | ||
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
[[Category: peptide]] | [[Category: peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:12 2008'' |
Revision as of 15:37, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALPHA-T-ALPHA, A DE NOVO DESIGNED PEPTIDE, NMR, 23 STRUCTURES
Overview
alpha t alpha is a 38-residue peptide designed to adopt a helical hairpin conformation in solution (Fezoui Y, Weaver DL Osterhout JJ, 1995, Protein Sci 4:286-295). A previous study of the carboxylate form of alpha t alpha by CD and two-dimensional NMR indicated that the peptide was highly helical and that the helices associated in approximately the intended orientation (Fezoui Y, Weaver DL, Osterhout JJ, 1994, Proc Natl Acad Sci USA 91:3675-3679). Here, the solution structure of alpha t alpha as determined by two-dimensional NMR is reported. A total of 266 experimentally derived distance restraints and 20 dihedral angle restraints derived from J-couplings were used. One-hundred initial structures were generated by distance geometry and refined by dynamical simulated annealing. Twenty-three of the lowest-energy structures consistent with the experimental restraints were analyzed. The results presented here show that alpha t alpha is comprised of two associating helices connected by a turn region.
About this Structure
1ABZ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of alpha t alpha, a helical hairpin peptide of de novo design., Fezoui Y, Connolly PJ, Osterhout JJ, Protein Sci. 1997 Sep;6(9):1869-77. PMID:9300486
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