2lgx
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | [[ | + | ==NMR structure for Kindle-2 N-terminus== |
+ | <StructureSection load='2lgx' size='340' side='right' caption='[[2lgx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | [[2lgx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGX OCA]. <br> | ||
+ | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Kindlin-2 belongs to an emerging class of regulators for heterodimeric (alpha/beta) integrin adhesion receptors. By binding to integrin beta cytoplasmic tail via its C-terminal FERM-like domain, kindlin-2 promotes integrin activation. Intriguingly, this activation process depends on the N terminus of kindlin-2 (K2-N) that precedes the FERM domain. The molecular function of K2-N is unclear. We present the solution structure of K2-N, which displays a ubiquitin fold similar to that observed in kindlin-1. Using chemical shift mapping and mutagenesis, we found that K2-N contains a conserved positively charged surface that binds to membrane enriched with negatively charged phosphatidylinositol-(4,5)-bisphosphate. We show that while wild-type kindlin-2 is capable of promoting integrin activation, such ability is significantly reduced for its membrane-binding defective mutant. These data suggest a membrane-binding function of the ubiquitin-like domain of kindlin-2, which is likely common for all kindlins to promote their localization to the plasma membrane and control integrin activation. | ||
- | + | Membrane Binding of the N-Terminal Ubiquitin-Like Domain of kindlin-2 Is Crucial for Its Regulation of Integrin Activation.,Perera HD, Ma YQ, Yang J, Hirbawi J, Plow EF, Qin J Structure. 2011 Nov 9;19(11):1664-71. PMID:22078565<ref>PMID:22078565</ref> | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | == | + | |
- | + | ||
- | + | ||
- | + | ||
- | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hirbawi, J.]] | [[Category: Hirbawi, J.]] |
Revision as of 08:18, 30 April 2014
NMR structure for Kindle-2 N-terminus
|
Categories: Homo sapiens | Hirbawi, J. | Ma, Y. | Perera, H D. | Plow, E F. | Qin, J. | Yang, J. | Cell adhesion | Integrin activation | Kindlin | Membrane