4um9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:26, 6 November 2024) (edit) (undo)
 
Line 9: Line 9:
</table>
</table>
== Disease ==
== Disease ==
-
[https://www.uniprot.org/uniprot/TGFB3_HUMAN TGFB3_HUMAN] Defects in TGFB3 are a cause of familial arrhythmogenic right ventricular dysplasia type 1 (ARVD1) [MIM:[https://omim.org/entry/107970 107970]; also known as arrhythmogenic right ventricular cardiomyopathy 1 (ARVC1). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall.<ref>PMID:15639475</ref>
+
[https://www.uniprot.org/uniprot/ITB6_HUMAN ITB6_HUMAN] Hypocalcified amelogenesis imperfecta;Hypoplastic amelogenesis imperfecta.
== Function ==
== Function ==
-
[https://www.uniprot.org/uniprot/TGFB3_HUMAN TGFB3_HUMAN] Involved in embryogenesis and cell differentiation.
+
[https://www.uniprot.org/uniprot/ITB6_HUMAN ITB6_HUMAN] Integrin alpha-V/beta-6 is a receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion.<ref>PMID:17545607</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Eight integrin alpha-beta heterodimers recognize ligands with an Arg-Gly-Asp (RGD) motif. However, the structural mechanism by which integrins differentiate among extracellular proteins with RGD motifs is not understood. Here, crystal structures, mutations and peptide-affinity measurements show that alphaVbeta6 binds with high affinity to a RGDLXXL/I motif within the prodomains of TGF-beta1 and TGF-beta3. The LXXL/I motif forms an amphipathic alpha-helix that binds in a hydrophobic pocket in the beta6 subunit. Elucidation of the basis for ligand binding specificity by the integrin beta subunit reveals contributions by three different betaI-domain loops, which we designate specificity-determining loops (SDLs) 1, 2 and 3. Variation in a pair of single key residues in SDL1 and SDL3 correlates with the variation of the entire beta subunit in integrin evolution, thus suggesting a paradigmatic role in overall beta-subunit function.
 +
 
 +
Structural determinants of integrin beta-subunit specificity for latent TGF-beta,Dong X, Hudson NE, Lu C, Springer TA Nat Struct Mol Biol. 2014 Nov 10. doi: 10.1038/nsmb.2905. PMID:25383667<ref>PMID:25383667</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4um9" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==

Current revision

Crystal structure of alpha V beta 6 with peptide

PDB ID 4um9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4um9"
Personal tools