We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2z21

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2z21.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2z21.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2z21| PDB=2z21 | SCENE= }}
{{STRUCTURE_2z21| PDB=2z21 | SCENE= }}
-
'''Crystal Structure of a five site mutated Cyanovirin-N'''
+
===Crystal Structure of a five site mutated Cyanovirin-N===
-
==Overview==
+
<!--
-
Cyanovirin-N (CV-N) is a 101 amino acid cyanobacterial lectin with potent antiviral activity against HIV, mediated by high-affinity binding to branched N-linked oligomannosides on the viral surface envelope protein gp120. The protein contains two carbohydrate-binding domains, A and B, each of which binds short oligomannosides independently in vitro. The interaction to gp120 could involve either a single domain or both domains simultaneously; it is not clear which mode would elicit the antiviral activity. The model is complicated by the formation of a domain-swapped dimer form, in which part of each domain is exchanged between two monomers, which contains four functional carbohydrate-binding domains. To clarify whether multivalent interactions with gp120 are necessary for the antiviral activity, we engineered a novel mutant, P51G-m4-CVN, in which the binding site on domain A has been knocked out; in addition, a [P51G] mutation prevents the formation of domain-swapped dimers under physiological conditions. Here, we present the crystal structures at 1.8 A of the free and of the dimannose-bound forms of P51G-m4-CVN, revealing a monomeric structure in which only domain B is bound to dimannose. P51G-m4-CVN binds gp120 with an affinity almost 2 orders of magnitude lower than wt CV-N and is completely inactive against HIV. The tight binding to gp120 is recovered in the domain-swapped version of P51G-m4-CVN, prepared under extreme conditions. Our findings show that the presence of at least two oligomannoside-binding sites, either by the presence of intact domains A and B or by formation of domain-swapped dimers, is essential for activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17636873}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17636873 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17636873}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Gp120]]
[[Category: Gp120]]
[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:50:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:48:09 2008''

Revision as of 15:48, 28 July 2008

Image:2z21.png

Template:STRUCTURE 2z21

Crystal Structure of a five site mutated Cyanovirin-N

Template:ABSTRACT PUBMED 17636873

About this Structure

2Z21 is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.

Reference

A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity., Fromme R, Katiliene Z, Giomarelli B, Bogani F, Mc Mahon J, Mori T, Fromme P, Ghirlanda G, Biochemistry. 2007 Aug 14;46(32):9199-207. Epub 2007 Jul 18. PMID:17636873

Page seeded by OCA on Mon Jul 28 18:48:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2z21"
Personal tools