1yik

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[[Image:1yik.gif|left|200px]]<br /><applet load="1yik" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yik.gif|left|200px]]
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caption="1yik, resolution 1.75&Aring;" />
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'''Structure of Hen egg white lysozyme soaked with Cu-cyclam'''<br />
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{{Structure
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|PDB= 1yik |SIZE=350|CAPTION= <scene name='initialview01'>1yik</scene>, resolution 1.75&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=MM1:1,4,8,11-TETRAAZA-CYCLOTETRADECANE CU(II)'>MM1</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]
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|GENE=
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}}
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'''Structure of Hen egg white lysozyme soaked with Cu-cyclam'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YIK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=MM1:'>MM1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIK OCA].
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1YIK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIK OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15701702 15701702]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15701702 15701702]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:23:19 2008''

Revision as of 13:23, 20 March 2008

Image:1yik.gif


PDB ID 1yik

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands: , , and
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



Structure of Hen egg white lysozyme soaked with Cu-cyclam


Overview

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.

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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