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.


1bp3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bp3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1bp3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bp3| PDB=1bp3 | SCENE= }}
{{STRUCTURE_1bp3| PDB=1bp3 | SCENE= }}
-
'''THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX'''
+
===THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX===
-
==Overview==
+
<!--
-
The human pituitary hormones, growth hormone (hGH) and prolactin (hPRL), regulate a large variety of physiological processes, among which are growth and differentiation of muscle, bone and cartilage cells, and lactation. These activities are initiated by hormone-receptor binding. The hGH and hPRL receptors (hGHR and hPRLR, respectively) are single-pass transmembrane receptors from class 1 of the haematopoietic receptor superfamily. This classification is based on sequence similarity in their extracellular domains, notably a highly conserved pentapeptide, the so-called 'WSXWS box', the function of which is controversial. All ligands in class 1 activate their respective receptors by clustering mechanisms. In the case of hGH, activation involves receptor homodimerization in a sequential process: the active ternary complex containing one ligand and two receptor molecules is formed by association of a receptor molecule to an intermediate 1:1 complex. hPRL does not bind to the hGH receptor, but hGH binds to both the hGHR and hPRLR, and mutagenesis studies have shown that the receptor-binding sites on hGH overlap. We present here the crystal structure of the 1:1 complex of hGH bound to the extracellular domain of the hPRLR. Comparisons with the hGH-hGHR complex reveal how hGH can bind to the two distinctly different receptor binding surfaces.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7984244}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7984244 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7984244}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Hormone/growth factor]]
[[Category: Hormone/growth factor]]
[[Category: Receptor]]
[[Category: Receptor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:47:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:29:05 2008''

Revision as of 16:29, 30 June 2008

Template:STRUCTURE 1bp3

THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX

Template:ABSTRACT PUBMED 7984244

About this Structure

1BP3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The X-ray structure of a growth hormone-prolactin receptor complex., Somers W, Ultsch M, De Vos AM, Kossiakoff AA, Nature. 1994 Dec 1;372(6505):478-81. PMID:7984244

Page seeded by OCA on Mon Jun 30 19:29:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools