Ligand recognition by the I domain-containing integrins

@article{Dickeson1998LigandRB,
  title={Ligand recognition by the I domain-containing integrins},
  author={S. Kent Dickeson and Samuel A. Santoro},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={1998},
  volume={54},
  pages={556-566}
}
Abstract. Seven of the integrin α subunits described to date, α1 , α2 , αL , αX , αd , αM and αE , contain a highly conserved I (or A) domain of approximately 200 amino acid residues inserted near the amino-terminus of the subunit. As the result of a variety of independent experimental approaches, a large body of data has recently accumulated that indicates that the I domains are independent, autonomously folding domains capable of directly binding ligands that play a necessary and important… Expand
Molecular Basis of Ligand Recognition by Integrin α5β1
TLDR
High-quality studies have shown that amino acid residues involved in ligand recognition by α5β1 can potentially be identified in gain-of-function experiments by their ability to switch the ligand binding properties of αVβ1 to those of α5 β1. Expand
Determinants of Ligand Binding Specificity of the α1β1 and α2β1Integrins*
TLDR
Structural components of the I domains responsible for the varying ligand specificities within the α1 and α2 integrin I domains reveal the existence of multiple determinants of ligand binding specificities. Expand
Multiple Binding Sites in Collagen Type I for the Integrins α1β1 and α2β1 *
Integrins α1β1 and α2β1 are two major collagen receptors on the surface of eukaryotic cells. Binding to collagen is primarily due to an A-domain near the N terminus of the α chains. Previously, weExpand
Salt-bridge modulates differential calcium-mediated ligand binding to integrin α1- and α2-I domains
TLDR
Data indicate the E152-R192 salt bridge is a key distinction in the molecular mechanism of differential ion binding of these two I domains, as reported to promote α1I but inhibit α2I ligand binding. Expand
Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experiment
TLDR
An NMR method is proposed, termed transferred cross-saturation (TCS), that enables the rigorous identification of contact residues in a huge protein complex, which allowed the successful determination of the ligand-binding site of the A3 domain. Expand
Cloning, sequence analysis, and chromosomal localization of the novel human integrin α11 subunit (ITGA11)
TLDR
The deduced α11 protein shows the typical structural features of integrin α-subunits and is similar to a distinct group of α- subunits from collagen-binding integrins, however, it differs from most integrinα-chains by an incompletely preserved cytoplasmic GFFKR motif. Expand
I. SPECIFICITY OF LIGAND BINDING IS DETERMINED BY AMINO ACID SEQUENCES IN THE SECOND AND THIRD NH2-TERMINAL REPEATS OF THE a SUBUNIT*
The NH2-terminal portion (putative ligand-binding domain) of a subunits contains 7 homologous repeats, the last 3 or 4 of which possess divalent cation binding sequences. These repeats are predictedExpand
Structural Analysis of the α2 Integrin I Domain/Procollagenase-1 (Matrix Metalloproteinase-1) Interaction*
TLDR
The α2 integrin/MMP-1 interaction described here extends an emerging paradigm in matrix biology involving anchoring of proteinases to the cell surface to regulate their biological activities. Expand
Structural determinants of the selectivity of KTS‐disintegrins for the α1β1 integrin
KTS‐disintegrins are a subfamily of short monomeric disintegrins that are potent and selective inhibitors of α1β1 integrin. The amino acid sequence of the new KTS‐disintegrin, viperistatin, differsExpand
α11β1 Integrin Recognizes the GFOGER Sequence in Interstitial Collagens*
TLDR
The data indicate that the GFOGER sequence in fibrillar collagens is a common recognition motif used by α1β1, α2 β1, and also α11β1 integrins, despite their distinct binding specificity for various collagen subtypes. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 92 REFERENCES
A Discrete Site Modulates Activation of I Domains
  • Li Zhang, E. Plow
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 1996
TLDR
The identification of a discrete site within the I domain of integrin αMβ2, which modulates the adhesive activity of this receptor, which represents a universal target for controlling integrin activation and the function of other I domain-containing proteins. Expand
The Integrin α1 A-domain Is a Ligand Binding Site for Collagens and Laminin*
TLDR
It is suggested that the A-domain is the major collagen binding site in the α1β1 and α2β1 integrins, and the first demonstration of laminin binding by A-domains is demonstrated. Expand
Two conformations of the integrin A-domain (I-domain): a pathway for activation?
TLDR
These observations provide the first atomic resolution view of conformational changes in an integrin domain, and suggest how these changes are linked to a change in integrin adhesiveness. Expand
Crystal structure of the A domain from the a subunit of integrin CR3 (CD11 b/CD18)
TLDR
The high resolution crystal structure of the A domain from the alpha chain of integrin CR3 is determined and it is suggested that the beta subunits of integrins contain a MIDAS motif within a modified A domain. Expand
The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin.
TLDR
The crystal structures of the CD11a I domain determined in the absence of bound metal ion and with bound magnesium ion indicate that the metal ion is either involved in direct interaction with ligand or required to promote a favorable quaternary arrangement of the integrin. Expand
Direct binding of collagen to the I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner.
TLDR
It is shown that the recombinant inserted/interactive domain (I domain) of alpha 2 specifically interacts with collagen, indicating the I domain contains all the components necessary for collagen binding. Expand
The role of the I domain in ligand binding of the human integrin alpha 1 beta 1.
TLDR
Analysis of potential ligand binding domains within the human integrin alpha 1 subunit suggests a central role for the I domain in ligand recognition for all integrinalpha subunits containing this domain. Expand
Contributions of the I and EF Hand Domains to the Divalent Cation-dependent Collagen Binding Activity of the α2β1 Integrin*
TLDR
Deletional analysis demonstrated that residues present within the amino-terminal 35 amino acids contribute to the 6F1 epitope and are required for Mg2+-dependent collagen binding and that the I domain alone is sufficient for collagen binding. Expand
Identification and Reconstruction of the Binding Site within αMβ2 for a Specific and High Affinity Ligand, NIF*
Engagement of the αMβ2 (CD11b/CD18, Mac-1) integrin on neutrophils supports adhesion and induces various cellular responses. These responses can be blocked by a specific ligand of αMβ2, neutrophilExpand
Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2,CD49b/CD29).
TLDR
The sequence of the residues 173-259 of alpha 2 overlap with the peptide sequences (M11 and M20) that derive from von Willebrand factor A1 and A3 domains (homologous to the alpha 2 I domain) and block von Wilrebrand factor/collagen interaction, suggesting that the epitope region ofalpha 2 may really be involved in ligand recognition. Expand
...
1
2
3
4
5
...