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.

1ehh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ehh.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ehh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ehh| PDB=1ehh | SCENE= }}
{{STRUCTURE_1ehh| PDB=1ehh | SCENE= }}
-
'''CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI COMPLEX WITH TRI-N-ACETYLCHITOTRIOSE'''
+
===CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI COMPLEX WITH TRI-N-ACETYLCHITOTRIOSE===
-
==Overview==
+
<!--
-
Urtica dioica agglutinin is a small plant lectin that binds chitin. We purified the isolectin VI (UDA-VI) and crystal structures of the isolectin and its complex with tri-N-acetylchitotriose (NAG3) were determined by X-ray analysis. The UDA-VI consists of two domains analogous to hevein and the backbone folding of each domain is maintained by four disulfide bridges. The sequence similarity of the two domains is not high (42 %) but their backbone structures are well superimposed except some loop regions. The chitin binding sites are located on the molecular surface at both ends of the dumbbell-shape molecule. The crystal of the NAG3 complex contains two independent molecules forming a protein-sugar 2:2 complex. One NAG3 molecule is sandwiched between two independent UDA-VI molecules and the other sugar molecule is also sandwiched by one UDA-VI molecule and symmetry-related another one. The sugar binding site of N-terminal domain consists of three subsites accommodating NAG3 while two NAG residues are bound to the C-terminal domain. In each sugar-binding site, three aromatic amino acid residues and one serine residue participate to the NAG3 binding. The sugar rings bound to two subsites are stacked to the side-chain groups of tryptophan or histidine and a tyrosine residue is in face-to-face contact with an acetylamino group, to which the hydroxyl group of a serine residue is hydrogen-bonded. The third subsite of the N-terminal domain binds a NAG moiety with hydrogen bonds. The results suggest that the triad of aromatic amino acid residues is intrinsic in sugar binding of hevein-like domains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10731420}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10731420 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10731420}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Muraki, M.]]
[[Category: Muraki, M.]]
[[Category: Two homologous hevein-like domain]]
[[Category: Two homologous hevein-like domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:06:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:42:27 2008''

Revision as of 21:42, 30 June 2008

Image:1ehh.png

Template:STRUCTURE 1ehh

CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI COMPLEX WITH TRI-N-ACETYLCHITOTRIOSE

Template:ABSTRACT PUBMED 10731420

About this Structure

1EHH is a Single protein structure of sequence from Urtica dioica. Full crystallographic information is available from OCA.

Reference

Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose., Harata K, Muraki M, J Mol Biol. 2000 Mar 31;297(3):673-81. PMID:10731420

Page seeded by OCA on Tue Jul 1 00:42:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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