1qgr: Difference between revisions

Revision as of 21:03, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qgr.png

Template:STRUCTURE 1qgr

STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)

Template:ABSTRACT PUBMED 10353244

About this StructureAbout this Structure

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

ReferenceReference

Structure of importin-beta bound to the IBB domain of importin-alpha., Cingolani G, Petosa C, Weis K, Muller CW, Nature. 1999 May 20;399(6733):221-9. PMID:10353244

Page seeded by OCA on Sun Jul 27 21:03:29 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qgr.gif|left|200px]]
+{{Seed}}
+[[Image:1qgr.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qgr|  PDB=1qgr  |  SCENE=  }}
-'''STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)'''
+===STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)===
-==Overview==
+<!--
-Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-alpha and importin-beta (also called karyopherin-alpha and -beta). The formation of this heterodimer involves the importin-beta-binding (IBB) domain of importin-alpha, a highly basic amino-terminal region of roughly 40 amino-acid residues. Here we report the crystal structure of human importin-beta bound to the IBB domain of importin-alpha, determined at 2.5 A and 2.3 A resolution in two crystal forms. Importin-beta consists of 19 tandemly repeated HEAT motifs and wraps intimately around the IBB domain. The association involves two separate regions of importin-beta, recognizing structurally distinct parts of the IBB domain: an amino-terminal extended moiety and a carboxy-terminal helix. The structure indicates that significant conformational changes occur when importin-beta binds or releases the IBB domain domain and suggests how dissociation of the importin-alpha/beta heterodimer may be achieved upon nuclear entry.
+The line below this paragraph, {{ABSTRACT_PUBMED_10353244}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10353244 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10353244}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Nuclear import]]
 [[Category: Transport receptor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:15:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:03:29 2008''