1gp3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1gp3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gp3, resolution 1.95&Aring;" /> '''HUMAN IGF2R DOMAIN ...)
Line 1: Line 1:
-
[[Image:1gp3.gif|left|200px]]<br />
+
[[Image:1gp3.gif|left|200px]]<br /><applet load="1gp3" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1gp3" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1gp3, resolution 1.95&Aring;" />
caption="1gp3, resolution 1.95&Aring;" />
'''HUMAN IGF2R DOMAIN 11'''<br />
'''HUMAN IGF2R DOMAIN 11'''<br />
==Overview==
==Overview==
-
Insulin-like growth factor II receptor (IGF2R) is a multifunctional cell, surface receptor implicated in tumour suppression. Its growth inhibitory, activity has been associated with an ability to bind IGF-II. IGF2R, contains 15 homologous extracellular domains, with domain 11 primarily, responsible for IGF-II binding. We report a 1.4 A resolution crystal, structure of domain 11, solved using the anomalous scattering signal of, sulfur. The structure consists of two crossed beta-sheets forming a, flattened beta-barrel. Structural analysis identifies the putative IGF-II, binding site at one end of the beta-barrel whilst crystal lattice contacts, suggest a model for the full-length IGF2R extracellular region. The, structure factors and coordinates of IGF2R domain 11 have been deposited, in the Protein Data Bank (accession codes 1GP0 and 1GP3).
+
Insulin-like growth factor II receptor (IGF2R) is a multifunctional cell surface receptor implicated in tumour suppression. Its growth inhibitory activity has been associated with an ability to bind IGF-II. IGF2R contains 15 homologous extracellular domains, with domain 11 primarily responsible for IGF-II binding. We report a 1.4 A resolution crystal structure of domain 11, solved using the anomalous scattering signal of sulfur. The structure consists of two crossed beta-sheets forming a flattened beta-barrel. Structural analysis identifies the putative IGF-II binding site at one end of the beta-barrel whilst crystal lattice contacts suggest a model for the full-length IGF2R extracellular region. The structure factors and coordinates of IGF2R domain 11 have been deposited in the Protein Data Bank (accession codes 1GP0 and 1GP3).
==Disease==
==Disease==
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
1GP3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GP3 OCA].
+
1GP3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GP3 OCA].
==Reference==
==Reference==
Line 18: Line 17:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brown, J.]]
[[Category: Brown, J.]]
-
[[Category: Esnouf, R.M.]]
+
[[Category: Esnouf, R M.]]
[[Category: Harlos, K.]]
[[Category: Harlos, K.]]
-
[[Category: Hassan, A.B.]]
+
[[Category: Hassan, A B.]]
-
[[Category: Jones, E.Y.]]
+
[[Category: Jones, E Y.]]
-
[[Category: Jones, M.A.]]
+
[[Category: Jones, M A.]]
[[Category: Linnell, J.]]
[[Category: Linnell, J.]]
[[Category: beta barrel]]
[[Category: beta barrel]]
Line 30: Line 29:
[[Category: transport]]
[[Category: transport]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:07:43 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:27 2008''

Revision as of 10:52, 21 February 2008


1gp3, resolution 1.95Å

Drag the structure with the mouse to rotate

HUMAN IGF2R DOMAIN 11

Contents

Overview

Insulin-like growth factor II receptor (IGF2R) is a multifunctional cell surface receptor implicated in tumour suppression. Its growth inhibitory activity has been associated with an ability to bind IGF-II. IGF2R contains 15 homologous extracellular domains, with domain 11 primarily responsible for IGF-II binding. We report a 1.4 A resolution crystal structure of domain 11, solved using the anomalous scattering signal of sulfur. The structure consists of two crossed beta-sheets forming a flattened beta-barrel. Structural analysis identifies the putative IGF-II binding site at one end of the beta-barrel whilst crystal lattice contacts suggest a model for the full-length IGF2R extracellular region. The structure factors and coordinates of IGF2R domain 11 have been deposited in the Protein Data Bank (accession codes 1GP0 and 1GP3).

Disease

Known diseases associated with this structure: Hepatocellular carcinoma OMIM:[147280]

About this Structure

1GP3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur., Brown J, Esnouf RM, Jones MA, Linnell J, Harlos K, Hassan AB, Jones EY, EMBO J. 2002 Mar 1;21(5):1054-62. PMID:11867533

Page seeded by OCA on Thu Feb 21 12:52:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools