Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
Fibronectin type III domains are found in many different proteins including cell surface receptors and cell adhesion molecules. The crystal structure of one such domain from the extracellular matrix protein tenascin was determined. The structure was solved by multiwavelength anomalous diffraction (MAD) phasing of the selenomethionyl protein and has been refined to 1.8 angstrom resolution. The folding topology of this domain is identical to that of the extracellular domains of the human growth hormone receptor, the second domain of CD4, and PapD. Although distinct, this topology is similar to that of immunoglobulin constant domains. An Arg-Gly-Asp (RGD) sequence that can function for cell adhesion is found in a tight turn on an exposed loop.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1992 |
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| Erschienen: |
1992 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:258 |
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| Enthalten in: |
Science (New York, N.Y.) - 258(1992), 5084 vom: 06. Nov., Seite 987-91 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Leahy, D J [VerfasserIn] |
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| Anmerkungen: |
Date Completed 23.12.1992 Date Revised 09.03.2022 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM01259900X |
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| 041 | |a eng | ||
| 100 | 1 | |a Leahy, D J |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein |
| 264 | 1 | |c 1992 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a Date Completed 23.12.1992 | ||
| 500 | |a Date Revised 09.03.2022 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Fibronectin type III domains are found in many different proteins including cell surface receptors and cell adhesion molecules. The crystal structure of one such domain from the extracellular matrix protein tenascin was determined. The structure was solved by multiwavelength anomalous diffraction (MAD) phasing of the selenomethionyl protein and has been refined to 1.8 angstrom resolution. The folding topology of this domain is identical to that of the extracellular domains of the human growth hormone receptor, the second domain of CD4, and PapD. Although distinct, this topology is similar to that of immunoglobulin constant domains. An Arg-Gly-Asp (RGD) sequence that can function for cell adhesion is found in a tight turn on an exposed loop | ||
| 650 | 4 | |a Comparative Study | |
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
| 650 | 4 | |a Research Support, U.S. Gov't, P.H.S. | |
| 650 | 7 | |a Cell Adhesion Molecules, Neuronal |2 NLM | |
| 650 | 7 | |a Extracellular Matrix Proteins |2 NLM | |
| 650 | 7 | |a Fibronectins |2 NLM | |
| 650 | 7 | |a Immunoglobulin Constant Regions |2 NLM | |
| 650 | 7 | |a Receptors, Somatotropin |2 NLM | |
| 650 | 7 | |a Recombinant Proteins |2 NLM | |
| 650 | 7 | |a Tenascin |2 NLM | |
| 700 | 1 | |a Hendrickson, W A |e verfasserin |4 aut | |
| 700 | 1 | |a Aukhil, I |e verfasserin |4 aut | |
| 700 | 1 | |a Erickson, H P |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Science (New York, N.Y.) |d 1880 |g 258(1992), 5084 vom: 06. Nov., Seite 987-91 |w (DE-627)NLM000023450 |x 1095-9203 |7 nnns |
| 773 | 1 | 8 | |g volume:258 |g year:1992 |g number:5084 |g day:06 |g month:11 |g pages:987-91 |
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| 952 | |d 258 |j 1992 |e 5084 |b 06 |c 11 |h 987-91 | ||