This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1len

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1len.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1len.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1len| PDB=1len | SCENE= }}
{{STRUCTURE_1len| PDB=1len | SCENE= }}
-
'''REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION'''
+
===REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
The structures of two crystal forms of lentil lectin are determined and refined at high resolution. Orthorhombic lentil lectin is refined at 1.80 A resolution to an R-factor of 0.184 and monoclinic lentil lectin at 1.75 A resolution to an R-factor of 0.175. These two structures are compared to each other and to the other available legume lectin structures. The monosaccharide binding pocket of each lectin monomer contains a tightly bound phosphate ion. This phosphate makes hydrogen bonding contacts with Asp-81 beta, Gly-99 beta, and Asn-125 beta, three residues that are highly conserved in most of the known legume lectin sequences and essential for monosaccharide recognition in all legume lectin crystal structures described thus far. A detailed analysis of the composition and properties of the hydrophobic contact network and hydrophobic nuclei in lentil lectin is presented. Contact map calculations reveal that dense clusters of nonpolar as well as polar side chains play a major role in secondary structure packing. This is illustrated by a large cluster of 24 mainly hydrophobic amino acids that is responsible for the majority of packing interactions between the two beta-sheets. Another series of four smaller and less hydrophobic clusters is found to mediate the packing of a number of loop structures upon the front sheet. A very dense, but not very conserved cluster is found to stabilize the transition metal binding site. The highly conserved and invariant nonpolar residues are distributed asymmetrically over the protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7731952}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7731952 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7731952}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
[[Category: Lectin]]
[[Category: Lectin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:51:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:19:49 2008''

Revision as of 21:19, 28 July 2008

Image:1len.png

Template:STRUCTURE 1len

REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 7731952

About this Structure

1LEN is a Protein complex structure of sequences from Lens culinaris. Full crystallographic information is available from OCA.

Reference

Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution., Loris R, Van Overberge D, Dao-Thi MH, Poortmans F, Maene N, Wyns L, Proteins. 1994 Dec;20(4):330-46. PMID:7731952

Page seeded by OCA on Tue Jul 29 00:19:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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