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1yik

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[[Image:1yik.gif|left|200px]]
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[[Image:1yik.png|left|200px]]
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{{STRUCTURE_1yik| PDB=1yik | SCENE= }}
{{STRUCTURE_1yik| PDB=1yik | SCENE= }}
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'''Structure of Hen egg white lysozyme soaked with Cu-cyclam'''
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===Structure of Hen egg white lysozyme soaked with Cu-cyclam===
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==Overview==
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The macrocyclic antiviral drug xylyl-bicyclam blocks entry of HIV into cells by targeting the CXCR4 coreceptor, a seven-helix transmembrane G-protein-coupled receptor. Its affinity for CXCR4 is enhanced by binding to Cu2+, Ni2+, or Zn2+. Metallocyclams have a rich configurational chemistry and proteins may bind selectively to specific metallocyclam configurations. Our studies of lysozyme reveal structural details of protein-metallocyclam interactions that are important for receptor recognition. Solution NMR studies show that Cu-cyclam interacts with specific tryptophan residues of lysozyme (Trp-62, Trp-63, and Trp-123). Two major binding sites for both Cu-cyclam and Cu2-xylyl-bicyclam were detected by x-ray crystallography. In the first site, Cu2+ in one cyclam ring of Cu2-xylyl-bicyclam adopts a trans configuration and is coordinated to a carboxylate oxygen of Asp-101, whereas for Cu-cyclam two ring NH groups form H bonds to the carboxylate oxygens of Asp-101, stabilizing an unusual cis (folded) cyclam configuration. For both complexes in this site, a cyclam ring is sandwiched between the indole side chains of two tryptophan residues (Trp-62 and Trp-63). In the second site, a trans cyclam ring is stacked on Trp-123 and H bonded to the backbone carbonyl of Gly-117. We show that there is a pocket in a model of the human CXCR4 coreceptor in which trans and cis configurations of metallobicyclam can bind by direct metal coordination to carboxylate side chains, cyclam-NH...carboxylate H bonding, together with hydrophobic interactions with tryptophan residues. These studies provide a structural basis for the design of macrocycles that bind stereospecifically to G-coupled and other protein receptors.
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(as it appears on PubMed at http://www.pubmed.gov), where 15701702 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15701702}}
==About this Structure==
==About this Structure==
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[[Category: Walkinshaw, M D.]]
[[Category: Walkinshaw, M D.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:27:13 2008''

Revision as of 23:27, 28 July 2008

Image:1yik.png

Template:STRUCTURE 1yik

Structure of Hen egg white lysozyme soaked with Cu-cyclam

Template:ABSTRACT PUBMED 15701702

About this Structure

1YIK is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Protein recognition of macrocycles: binding of anti-HIV metallocyclams to lysozyme., Hunter TM, McNae IW, Liang X, Bella J, Parsons S, Walkinshaw MD, Sadler PJ, Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2288-92. Epub 2005 Feb 8. PMID:15701702

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