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.


1a2k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a2k.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a2k.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a2k| PDB=1a2k | SCENE= }}
{{STRUCTURE_1a2k| PDB=1a2k | SCENE= }}
-
'''GDPRAN-NTF2 COMPLEX'''
+
===GDPRAN-NTF2 COMPLEX===
-
==Overview==
+
<!--
-
Nuclear transport factor 2 (NTF2) and the Ras-family GTPase Ran are two soluble components of the nuclear protein import machinery. NTF2 binds GDP-Ran selectively and this interaction is important for efficient nuclear protein import in vivo. We have used X-ray crystallography to determine the structure of the macromolecular complex formed between GDP-Ran and nuclear transport factor 2 (NTF2) at 2.5 A resolution. The interaction interface involves primarily the putative switch II loop of Ran (residues 65 to 78) and the hydrophobic cavity and surrounding surface of NTF2. The major contribution to the interaction made by the switch II loop accounts for the ability of NTF2 to discriminate between GDP and GTP-bound forms of Ran. The aromatic side-chain of Ran Phe72 inserts into the NTF2 cavity and accounts for 22% of the surface area buried by the interaction interface, while salt bridges are formed between Lys71 and Arg76 of Ran with Asp92/Asp94 and Glu42 of NTF2, respectively. These salt bridges account for the inhibition of the Ran-NTF2 interaction by NTF2 mutants such as E42 K and D92/94N in which the negatively charged residues surrounding the cavity were altered. Because the interaction interface maintains the positions of key Ran residues involved in binding MgGDP, NTF2 binding may help stabilize the switch state of Ran, possibly in the context of targeting it to other components of the nuclear protein import machinery to specify directionality of transport. The binding of GDP-Ran at the NTF2 cavity raises the possibility that this interaction might be modulated by a metabolite or small molecule substrate for NTF2's putative enzymatic activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9533885}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9533885 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9533885}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Stewart, M.]]
[[Category: Stewart, M.]]
[[Category: Gtp-binding]]
[[Category: Gtp-binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:42:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:51:33 2008''

Revision as of 12:51, 30 June 2008

Image:1a2k.png

Template:STRUCTURE 1a2k

GDPRAN-NTF2 COMPLEX

Template:ABSTRACT PUBMED 9533885

About this Structure

1A2K is a Protein complex structure of sequences from Canis lupus familiaris and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran., Stewart M, Kent HM, McCoy AJ, J Mol Biol. 1998 Apr 3;277(3):635-46. PMID:9533885

Page seeded by OCA on Mon Jun 30 15:51:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a2k"
Personal tools