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.

1lho

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lho.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lho.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lho| PDB=1lho | SCENE= }}
{{STRUCTURE_1lho| PDB=1lho | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE N-TERMINAL LG-DOMAIN OF SHBG IN COMPLEX WITH 5ALPHA-ANDROSTANE-3BETA,17BETA-DIOL'''
+
===CRYSTAL STRUCTURE OF THE N-TERMINAL LG-DOMAIN OF SHBG IN COMPLEX WITH 5ALPHA-ANDROSTANE-3BETA,17BETA-DIOL===
-
==Overview==
+
<!--
-
The amino-terminal laminin G-like domain of human sex hormone-binding globulin (SHBG) contains a single high affinity steroid-binding site. Crystal structures of this domain in complex with several different steroid ligands have revealed that estradiol occupies the SHBG steroid-binding site in an opposite orientation when compared with 5 alpha-dihydrotestosterone or C19 androgen metabolites (5 alpha-androstan-3 beta,17 beta-diol and 5 alpha-androstan-3 beta,17 alpha-diol) or the synthetic progestin levonorgestrel. Substitution of specific residues within the SHBG steroid-binding site confirmed that Ser(42) plays a key role in determining high affinity interactions by hydrogen bonding to functional groups at C3 of the androstanediols and levonorgestrel and the hydroxyl at C17 of estradiol. Among residues participating in the hydrogen bond network with hydroxy groups at C17 of C19 steroids or C3 of estradiol, Asp(65) appears to be the most important. The different binding mode of estradiol is associated with a difference in the position/orientation of residues (Leu(131) and Lys(134)) in the loop segment (Leu(131)-His(136)) that covers the steroid-binding site as well as others (Leu(171)-Lys(173) and Trp(84)) on the surface of human SHBG and may provide a basis for ligand-dependent interactions between SHBG and other macromolecules. These new crystal structures have also enabled us to construct a simple space-filling model that can be used to predict the characteristics of novel SHBG ligands.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12065592}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12065592 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12065592}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: 17b-dha]]
[[Category: 17b-dha]]
[[Category: Shbg]]
[[Category: Shbg]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:55:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:56:11 2008''

Revision as of 17:56, 2 July 2008

Image:1lho.png

Template:STRUCTURE 1lho

CRYSTAL STRUCTURE OF THE N-TERMINAL LG-DOMAIN OF SHBG IN COMPLEX WITH 5ALPHA-ANDROSTANE-3BETA,17BETA-DIOL

Template:ABSTRACT PUBMED 12065592

About this Structure

1LHO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation., Grishkovskaya I, Avvakumov GV, Hammond GL, Catalano MG, Muller YA, J Biol Chem. 2002 Aug 30;277(35):32086-93. Epub 2002 Jun 13. PMID:12065592

Page seeded by OCA on Wed Jul 2 20:56:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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