Three-dimensional structure of cell adhesion molecules

Current Opinion in Cell Biology

Volumn 8, Issue 5, 1996, Pages 602-608

  Yvonne Jones, E ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; CARBOHYDRATE BINDING PROTEIN; CELL ADHESION MOLECULE; FIBRONECTIN; INTEGRIN; VASCULAR CELL ADHESION MOLECULE 1;

CELL ADHESION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 0030272010     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80100-1     Document Type: Article

References (50)

1. Campbell ID, Spitzfaden C: Building proteins with fibronectin type III modules. Structure 1994, 2:333-337.
2. Vaughn DE, Bjorkman PJ: The (greek) key to structures of neural adhesion molecules. Neuron 1996, 16:261-273.
3. Stuart Dl, Jones EY: Recognition at the cell surface: recent structural insights. Curr Opin Struct Biol 1995, 5:735-743.
4. Jones EY, Davis SJ, Williams AF, Marios K, Stuart Dl: Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Nature 1992, 360:232-239.
5. Bodian DL, Jones EY, Harlos K, Stuart Dl, Davis SJ: Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution. Structure 1994, 2:755-766.
6. Van der Merwe P, McNamee PN, Davies EA, Barclay AN, Davis SJ: Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells. Curr Biol 1995, 5:74-84. Describes the elegant use of complementary mutagenesis in rat CD2 and CD48 to confirm the geometry of the adhesive interface first proposed on the basis of lattice contacts in the rat CD2 crystal structure.
7. Nose A, Tsuji K, Takeichi M: Localization of specificity determining sites in cadherin cell-adhesion molecules. Cell 1990, 61:147-155.
8. Overduin M, Harvey TS, Bagby S, long KI, Yau P, Takeichi M, Ikura M: Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science 1995, 267:386-389. Of note as the first detailed structural information on E-cadherin.
9. Shapiro L, Fannon AM, Kwong PD, Thomson A, Lehmann MS, Grubel G, Legrand JF, Alsnielsen J, Colman DR, Hendrickson WA: Structural basis of cell-cell adhesion by cadherins. Nature 1995, 374:306-307. In addition to providing the first detailed structural information on N-cadherin, this paper is of particular interest both because of the implications for dimerization and because of the information on adhesive interactions that is drawn from lattice contacts in a series of three different crystals.
10. Shapiro L, Kwong PD, Fannon AM, Colman DR, Hendrickson WA: Considerations on the folding topology and evolutionary origin of cadherin domains. Proc Natl Acad Sci USA 1995, 92:6793-6797. A paper which complements [9), with further details on the structure of the cadherin fold and discussion of its relationship to similar topologies such as the Ig fold.
11. 2+-binding site and providing fresh implications for the overall architecture of the E-cadherin molecule.
12. Tomschy A, Fauser C, Landwehr R, Engel J: Homophilic adhesion of E-cadherin occurs by a cooperative two-step interaction of N-terminal domains. EMBO J 1996, in press. Intriguing data from electron microscopy on the nature of E-cadherin dimerization and adhesion.
13. Ruoslahti E, Pierschbacher MD: New perspectives in cell adhesion: ROD and integrins. Science 1987, 238:491-497.
14. Lee JO, Rieu P, Arnaout MA, Liddington R: Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18). Cell 1995, 80:631-638. An important paper which provides the first structure of an integrin I domain and reveals the functional MIDAS motif.
15. Lee J-O, Bankston LA, Arnaout MA, Liddington RC: Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure 1995, 3:1333-1340. A second Mac-1 I-domain structure from the authors of [14]. The paper reports an alternative metal coordination and significant changes in I-domain structure from which the authors, rather controversially, postulate the mechanism of activation of Mac-1.
16. 2) integrin. Proc Natl Acad Sci USA 1995, 92:10277-10281. Reports the structure of the l-domain of a second integrin, namely LFA-1. The authors take an opposing stance to that of the authors of [14,15] on the nature of the active I-domain structure. The debate will doubtless continue until substantially more structural information is available on the integrins.
17. Huang C, Springer TA: A binding Interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1). J Biol Chem 1995, 270:19008-19016. The authors seize the chance to map mutagenesis data on an I-domain structure, with very satisfying results.
18. Edwards CP, Champe M, Gonzalez T, Wessinger ME, Spencer SA, Presta LG, Berman PW, Bodary SC: Identification of amino acids in the CD11a I-domain important for binding of the leukocyte function-associated antigen-1 (LFA-1) to intercellular adhesion molecule-1 (ICAM-1). J Biol Chem 1995, 270:12635-12640. Describes mutagenesis data essential in building up an understanding of the functionally important elements of the I domain. See also [19].
19. Kamata T, Wright R, Takada Y: Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi. J Biol Chem 1995, 270:12531-12535. See annotation [18].
20. Main AL, Harvey TS, Baron M, Boyd J, Campbell ID: The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 1992,71:671-678.
21. Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP: Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 1992, 258:987-991.
22. Dickinson CD, Veerapandian B, Da XP, Hamlin RC, Xuong NH, Ruoslahti E, Ely KR: Crystal structure of the tenth type III cell adhesion module of human fibronectin. J Mol Biol 1994, 236:1079-1092.
23. Huber AH, Wang YM, Bieter AJ, Bjorkman PJ: Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0Å. Neuron 1994, 12:717-731.
24. Logan D, Abu-Ghazaleh R, Blakemore W, Curry S, Jackson T, King A, Lea S, Lewis R, Newman J, Stuart D, Fry E: Structure of a major immunogenic site on foot-and-mouth disease virus. Nature 1993, 362:566-568.
25. Jones EY, Harlos K, Bottomley MJ, Robinson RC, Driscoll PC, Edwards RM, Clements JM, Dudgeon TJ Stuart DI: Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule 1 (VCAM-1) at 1.8 Åresolution. Nature 1995, 373:539-544. First insights into the structural features which allow certain molecules of the IgSF to bind integrins. See also [26].
26. Wang JH, Pepinsky RB, Stehle T, Liu JH, Karpusas M, Browning B, Osborn L: The crystal structure of an N-terminal 2-domain fragment of vascular cell-adhesion molecule-1 (VCAM-1): a cyclic peptide-based on the domain-1 C-D loop can inhibit VCAM-1/α4 integrin interaction. Proc Natl Acad Sci USA 1995, 92:5714-5718. See annotation [25].
27. 7 under different activity states. J Immunol 1995, 155:5257-5267. Describes mutagenesis data essential in building up an understanding of the functionally important elements in members of the IgSF which bind integrins. See also [28,29].
28. 7. J Immunol 1996, 156:719-726. See annotation [27].
29. Holness CL, Bates PA, Littler AJ, Buckley CD, McDowall A, Bossy D, Hogg N, Simmons DL: Analysis of the binding-site on intercellular-adhesion molecule-3 for the leukocyte integrin lymphocyte function-associated antigen-1. J Biol Chem 1995, 270:877-884. See annotation [27].
30. 1 J Cell Biol 1994, 125:1395-1406.
31. 1). J Cell Biol 1994, 124:601-608.
32. Vonderheide RH, Tedder TF, Springer TA, Staunton DE: Residues within a conserved amino acid motif of domains 1 and 4 of VCAM-1 are required for binding to VLA-4. J Cell Biol 1994, 125:215-222.
33. Clements JM, Newham P, Shepherd M, Gilbert R, Dudgeon TJ, Needham LA, Edwards RM, Berry L, Brass A, Humphries MJ: Identification of a key integrin-binding sequence in VCAM-1 homologous to the LDV active-site in fibronectin. J Cell Sci 1994, 107:2127-2135.
34. Leahy DJ, Aukhil I, Erickson HP: 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996, 84:155-164. A very interesting paper presenting the first detailed structural information on a fragment of more than two domains (in this case four) of a multidomain adhesion molecule. The paper reveals the relative orientation of two separate sites implicated in integrin-mediated cell adhesion.
35. Aota S, Nagai T, Yamada KM: Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. J Biol Chem 1991, 266:15938-15943.
36. Aota S, Nomizu M, Yamada KM: The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function J Biol Chem 1994, 269:24756-24761.
37. a (platelet GPIIb-IIIa) recognizes multiple sites in fibronectin. J Biol Chem 1991, 266:23323-23328.
38. 3 integrins. J Biol Chem 1994, 269:10856-10863.
39. Rosen SD, Bertozzi CR: The selectins and their ligands. Curr Opin Cell Biol 1994, 6:663-673.
40. Graves BJ, Crowther RL, Chandran C, Rumberger JM, Li S, Huang K-S, Presky DH, Familletti PC, Wolitzky BA, Burns DK: Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains. Nature 1994, 367:532-538.
41. Weis WI, Drickamer K: Structural basis of lectin-carbohydrate recognition. Annu Rev Biochem 1996, 65:441-473.
42. Blanck O, lobst ST, Gabel C, Drickamer K: Introduction of selectin-like binding-specificity into a homologous mannosebinding protein. J Biol Chem 1996, 271:7289-7292. An elegant demonstration of transplanting functional specificity between homologous structural scaffolds.
43. Alon R, Hammer DA, Springer TA: Lifetime of the P-selectin-carbohydrate bond and its response to tensile force in hydrodynamic flow. Nature 1995, 374:539-542. Describes an innovative use of macroscopic biophysical measurements to probe the characteristics of cell adhesion interactions. See also [44].
44. Finger EB, Puri KD, Alon R, Lawrence MB, Von Andrian UH, Springer TA: Adhesion through L-selectin requires a threshold hydrodynamic shear. Nature 1996, 379:266-269. See annotation [43].
45. Powell LD, Varki A: I-type lectins. J Biol Chem 1995, 270:14243-14246.
46. Keim S, Pelz A, Schauer R, Filbin MT, Tang S, Debellard ME, Schnaar RL, Mahoney JA, Hartnell A, Bradfield P, Crocker PR: Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. Curr Biol 1994, 4:965-972.
47. Vinson M, Van der Merwe PA, Keim S, May A, Jones EY, Crocker PR: Characterization of the sialic acid-binding site in Sialoadhesin by site-directed mutagenesis. J Biol Chem 1996, 271:9267-9272. Presents mutagenesis data essential in building up an understanding of the functionally important elements in members of the IgSF which bind sialic acid. See also [48].
48. Van Der Merwe PA, Crocker PR, Vinson M, Barclay AN, Schauer R, Keim S: Localization of the putative sialic acid-binding site on the immunoglobulin superfamily cell-surface molecule CD22. J Biol Chem 1996, 271:9273-9280. See annotation [47].
49. 3 integrin involved in adhesion of leukocytes to endothelium. J Cell Biol 1995, 130:451-460. A classic example of the current trend for discovering additional modes of interaction mediated by established adhesion molecules. See also [50].
50. 3 as a heterotypic ligand for CD31/PECAM-1. J Cell Sci 1996, 109:437-445. See annotation [49].