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.


1yzm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yzm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1yzm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yzm| PDB=1yzm | SCENE= }}
{{STRUCTURE_1yzm| PDB=1yzm | SCENE= }}
-
'''Structure of Rabenosyn (458-503), Rab4 binding domain'''
+
===Structure of Rabenosyn (458-503), Rab4 binding domain===
-
==Overview==
+
<!--
-
Rab GTPases regulate all stages of membrane trafficking, including vesicle budding, cargo sorting, transport, tethering and fusion. In the inactive (GDP-bound) conformation, accessory factors facilitate the targeting of Rab GTPases to intracellular compartments. After nucleotide exchange to the active (GTP-bound) conformation, Rab GTPases interact with functionally diverse effectors including lipid kinases, motor proteins and tethering complexes. How effectors distinguish between homologous Rab GTPases represents an unresolved problem with respect to the specificity of vesicular trafficking. Using a structural proteomic approach, we have determined the specificity and structural basis underlying the interaction of the multivalent effector rabenosyn-5 with the Rab family. The results demonstrate that even the structurally similar effector domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions. The observed specificity is determined at a family-wide level by structural diversity in the active conformation, which governs the spatial disposition of critical conserved recognition determinants, and by a small number of both positive and negative sequence determinants that allow further discrimination between Rab GTPases with similar switch conformations.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16034420}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16034420 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16034420}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Rabenosyn]]
[[Category: Rabenosyn]]
[[Category: Vesicular trafficking]]
[[Category: Vesicular trafficking]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:00:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:14:34 2008''

Revision as of 08:14, 29 July 2008

Image:1yzm.png

Template:STRUCTURE 1yzm

Structure of Rabenosyn (458-503), Rab4 binding domain

Template:ABSTRACT PUBMED 16034420

About this Structure

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

Reference

Structural basis of family-wide Rab GTPase recognition by rabenosyn-5., Eathiraj S, Pan X, Ritacco C, Lambright DG, Nature. 2005 Jul 21;436(7049):415-9. PMID:16034420

Page seeded by OCA on Tue Jul 29 11:14:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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