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.

1zhq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zhq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zhq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zhq| PDB=1zhq | SCENE= }}
{{STRUCTURE_1zhq| PDB=1zhq | SCENE= }}
-
'''Crystal structure of apo MVL'''
+
===Crystal structure of apo MVL===
-
==Overview==
+
<!--
-
The cyanobacterial protein MVL inhibits HIV-1 envelope-mediated cell fusion at nanomolar concentrations by binding to high mannose N-linked carbohydrate on the surface of the envelope glycoprotein gp120. Although a number of other carbohydrate-binding proteins have been shown to inhibit HIV-1 envelope-mediated cell fusion, the specificity of MVL is unique in that its minimal target comprises the Man(alpha)(1--&gt;6)Man(beta)(1--&gt;4)GlcNAc(beta)(1--&gt;4)GlcNAc tetrasaccharide core of oligomannosides. We have solved the crystal structures of MVL free and bound to the pentasaccharide Man3GlcNAc2 at 1.9- and 1.8-A resolution, respectively. MVL is a homodimer stabilized by an extensive intermolecular interface between monomers. Each monomer contains two structurally homologous domains with high sequence similarity connected by a short five-amino acid residue linker. Intriguingly, a water-filled channel is observed between the two monomers. Residual dipolar coupling measurements indicate that the structure of the MVL dimer in solution is identical to that in the crystal. Man3GlcNAc2 binds to a preformed cleft at the distal end of each domain such that a total of four independent carbohydrate molecules associate with each homodimer. The binding cleft provides shape complementarity, including the presence of a deep hydrophobic hole that accommodates the N-acetyl methyl at the reducing end of the carbohydrate, and specificity arises from 7-8 intermolecular hydrogen bonds. The structures of MVL and the MVL-Man3GlcNAc2 complex further our understanding of the molecular basis of high affinity and specificity in protein-carbohydrate recognition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15937331}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15937331 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15937331}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hiv-1]]
[[Category: Hiv-1]]
[[Category: Mvl]]
[[Category: Mvl]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:38:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:02:18 2008''

Revision as of 21:02, 27 July 2008

Image:1zhq.png

Template:STRUCTURE 1zhq

Crystal structure of apo MVL

Template:ABSTRACT PUBMED 15937331

About this Structure

1ZHQ is a Single protein structure of sequence from Microcystis viridis. Full crystallographic information is available from OCA.

Reference

Crystal structures of the HIV-1 inhibitory cyanobacterial protein MVL free and bound to Man3GlcNAc2: structural basis for specificity and high-affinity binding to the core pentasaccharide from n-linked oligomannoside., Williams DC Jr, Lee JY, Cai M, Bewley CA, Clore GM, J Biol Chem. 2005 Aug 12;280(32):29269-76. Epub 2005 Jun 3. PMID:15937331

Page seeded by OCA on Mon Jul 28 00:02:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zhq"
Personal tools