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| - | [[Image:1slf.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1slf.png|left|200px]] |
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| | {{STRUCTURE_1slf| PDB=1slf | SCENE= }} | | {{STRUCTURE_1slf| PDB=1slf | SCENE= }} |
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| - | '''APOSTREPTAVIDIN, PH 5.6, TWO MOLECULES OF (SO4)2 BOUND AT THE BIOTIN BINDING SITE'''
| + | ===APOSTREPTAVIDIN, PH 5.6, TWO MOLECULES OF (SO4)2 BOUND AT THE BIOTIN BINDING SITE=== |
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| - | ==Overview==
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| - | The streptavidin-bound crystal structures of two disulfide-bridge cyclic peptides (cyclo-Ac-[CHPQGPPC]-NH2 and cyclo-Ac-[CHPQFC]-NH2) and of a linear peptide (FSHPQNT) were determined, as well as the structure of apostreptavidin (streptavidin-sulfate). Both the linear and disulfide-bridged cyclic peptides studied share a common HPQ conformation and make common interactions with streptavidin, although significant differences in structures and interactions occur for flanking residues among the complexes. The conformation of the linear peptide in the crystal structure of streptavidin-FSHPQNT was found to differ from that in the same complex published [Weber, P. C., Pantoliano, M. W., & Thompson, L. D. (1992) Biochemistry 31, 9350-9354]. In the present investigation, the HPQNT portion of the ligand is well-defined with some density defining the Phe, whereas in the investigation of Weber et al. only the HPQ segment of the bound peptide could be interpreted. Both bound cyclic peptides adopt a beta-turn involving an H-bond between the His main chain carbonyl and the main chain amide NH of the i+3 residue. In the streptavidin-bound cyclo-Ac-[CHPQFC]-NH2 structure, there is an additional H-bond, indicative of alpha-helix, between the main chain His carbonyl and the main chain C-terminal Cys amide NH group. Binding interactions for both cyclic and linear peptides include direct H-bonds, H-bonds mediated by tightly bound water molecules, and hydrophobic interactions. The above structures and that of streptavidin-biotin in the literature are compared and discussed in the context of structure-based ligand design. | + | The line below this paragraph, {{ABSTRACT_PUBMED_7492542}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7492542 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7492542}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Katz, B A.]] | | [[Category: Katz, B A.]] |
| | [[Category: Biotin-binding protein]] | | [[Category: Biotin-binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:51:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:26:51 2008'' |
Revision as of 01:26, 29 July 2008
Template:STRUCTURE 1slf
APOSTREPTAVIDIN, PH 5.6, TWO MOLECULES OF (SO4)2 BOUND AT THE BIOTIN BINDING SITE
Template:ABSTRACT PUBMED 7492542
About this Structure
1SLF is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.
Reference
Binding to protein targets of peptidic leads discovered by phage display: crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence., Katz BA, Biochemistry. 1995 Nov 28;34(47):15421-9. PMID:7492542
Page seeded by OCA on Tue Jul 29 04:26:51 2008
